TODO: Add description for P10928
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0019076
viral release from host cell
|
IEA
GO_REF:0000002 |
PENDING |
Summary: TODO: Review this GOA annotation
|
|
GO:0098003
viral tail assembly
|
IEA
GO_REF:0000043 |
PENDING |
Summary: TODO: Review this GOA annotation
|
|
GO:0098015
virus tail
|
IEA
GO_REF:0000043 |
PENDING |
Summary: TODO: Review this GOA annotation
|
|
GO:0098025
virus tail, baseplate
|
IEA
GO_REF:0000120 |
PENDING |
Summary: TODO: Review this GOA annotation
|
|
GO:0098025
virus tail, baseplate
|
IDA
PMID:27193680 Structure of the T4 baseplate and its function in triggering... |
PENDING |
Summary: TODO: Review this GOA annotation
|
The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The research target is Enterobacteria phage T4 gene product 10 (gp10), UniProt P10928, described in primary literature as a 602-aa trimeric baseplate wedge protein that is part of the T4 tail baseplate and is distinct from “gp10” designations in other phages (where “gp10” can refer to unrelated proteins such as tail tube subunits). This identity matches multiple independent T4 structural and biochemical studies that explicitly localize gp10 within the T4 baseplate wedge/pin region and report its trimeric state and 18-copy stoichiometry in the virion. (arisaka2016molecularassemblyand pages 1-2, leiman2006evolutionofbacteriophage pages 1-3)
The T4 baseplate is a multi-protein assembly at the distal end of the contractile tail that acts as a signaling and mechanical transducer: receptor engagement by tail fibers leads to a conformational transition of the baseplate that is coupled to tail sheath contraction. Structurally, the baseplate is composed of a central hub surrounded by six identical wedges. (yap2016roleofbacteriophage pages 1-3, arisaka2016molecularassemblyand pages 2-4)
gp10 is not an enzyme and no catalytic reaction/substrate specificity is reported for it in the retrieved evidence; instead, gp10 is best understood as a structural adaptor and mechanical “lever” protein in the baseplate wedge. Its function is mediated through specific protein–protein interfaces (notably with gp7, gp11, gp12, and gp9) and through large domain reorientations during baseplate activation. (leiman2006evolutionofbacteriophage pages 1-3, yap2016roleofbacteriophage pages 1-3)
gp10 is a virion structural protein located in the baseplate wedge/pin region at the tail tip, external to the host prior to infection. In cryo-EM reconstructions of the T4 baseplate, gp10 density lies at each hexagonal vertex/wedge where it is clamped by gp11 and contacts a short tail fiber (gp12). (kostyuchenko2003threedimensionalstructureof pages 2-3)
High-resolution structural work describes gp10 as a 602-residue trimeric protein organized into four domains, each forming a homotrimer, with non-collinear trimer axes that allow substantial reorientation during baseplate conformational switching. (yap2016roleofbacteriophage pages 1-3)
Domain-level functional assignments (structure-based):
- Domain I (N-terminus) includes a trimeric coiled-coil (residues 1–39) that binds the C-terminal region of gp7, physically integrating gp10 into the wedge backbone. (yap2016roleofbacteriophage pages 1-3)
- Domain II acts as an adaptor for short tail fibers (STFs), gp12, providing a direct STF binding interface. (yap2016roleofbacteriophage pages 1-3)
- Domain III provides an attachment site for gp11, placing gp10 at the gp11-associated vertex where fiber/baseplate interfaces converge. (yap2016roleofbacteriophage pages 1-3)
- Domain IV (C-terminus) contacts gp7 and gains additional contacts with gp9 in the activated star state. (yap2016roleofbacteriophage pages 1-3)
These interfaces collectively support a functional model in which gp10 is a connector among the gp7 wedge backbone, the gp11 vertex structure, and the gp12 short tail fibers, while also engaging gp9 upon activation. (yap2016roleofbacteriophage pages 1-3, leiman2006evolutionofbacteriophage pages 3-5)
Multiple sources report gp10 stoichiometry as 18 copies total, consistent with 3 subunits per wedge × 6 wedges. (arisaka2016molecularassemblyand pages 1-2, arisaka2013proteininteractionsin pages 2-4)
Independent cryo-EM density/volume reasoning also supports a gp10 trimer in the pin/wedge density, where gp11:gp10:gp7 is inferred as 3:3:1 at a vertex/wedge region. (kostyuchenko2003threedimensionalstructureof pages 2-3)
Biochemical reconstitution and analytical ultracentrifugation show that gp10 participates in the earliest baseplate wedge assembly steps, forming defined intermediates:
- A gp10–gp11 wedge initiation complex is a heterohexamer (gp10)3(gp11)3 with measured molecular weight 284,000 ± 7,000 Da and s20,w = 9.01 S, and it is elongated (frictional ratio ~1.7), consistent with a structural pin-like component rather than a compact globular complex. (zhao2000stoichiometryandintersubunit pages 5-7)
- Sequential assembly intermediates detected by sedimentation velocity include: gp10–gp7 (10.2 S), gp10–gp7–gp8 (12.1 S), gp10–gp7–gp8–gp6 (14.5 S), gp10–gp7–gp8–gp6–gp53 (15.0 S), and gp10–gp7–gp8–gp6–gp53–gp25 (15.3 S). (yap2010sequentialassemblyof pages 3-5)
- A gp10-containing wedge intermediate (~15.0 S) can spontaneously associate into a hubless, baseplate-like star at 43.7 S, indicating that gp10-containing wedge modules are sufficient (with partner proteins) to build a major activated-state-like assembly in vitro. (yap2010sequentialassemblyof pages 3-5)
Mechanistically, this supports a functional annotation of gp10 as an assembly nucleator and structural organizer rather than a late accessory protein. (yap2010sequentialassemblyof pages 3-5, arisaka2016molecularassemblyand pages 2-4)
The T4 baseplate switches from a high-energy “dome” (pre-attachment) to a lower-energy “star” (post-attachment) conformation, a key step preceding/associated with tail sheath contraction. gp10 is directly implicated by structural fitting into both conformations:
- In a crystallography + cryo-EM fitting study, the whole gp10 rotates ~100° about its long axis, and domain IV rotates ~60° during the hexagon→star transition. (leiman2006evolutionofbacteriophage pages 1-3)
- During this transition gp10 changes binding partners, losing contact with the C-terminal region of gp12 and gaining contact with gp9, while maintaining contact with gp7. (leiman2006evolutionofbacteriophage pages 3-5)
These observations support the interpretation that gp10 contributes to the mechanical rearrangement at the baseplate periphery that couples fiber engagement to global baseplate remodeling. (leiman2006evolutionofbacteriophage pages 1-3, leiman2006evolutionofbacteriophage pages 3-5)
In a Nature study of baseplate structure/function, removal of the covalent linkage between gp7 and gp10 is reported to profoundly reduce infectivity, with the authors concluding that the bond is important for maintaining baseplate structure during the conformational switch. (taylor2016structureofthe pages 3-6)
In the same study, a gp7 C184A mutant reduced titer by approximately ~20-fold in plaque assays, consistent with the idea that specific chemical/structural features at or near the gp7–gp10 interface are important for infection efficiency even when gross virion morphology appears WT by cryo-EM. (taylor2016structureofthe pages 3-6)
Cryo-EM reconstructions in pre- and post-attachment states provide quantitative evidence for conformational switching:
- Pre-attachment: 37,913 particles, 4.11 Å reconstruction.
- Post-attachment: 5,176 particles, 6.77 Å reconstruction.
Differences in resolution and alignment uncertainty (rotation parameter accuracies ~0.267° vs ~0.695°) are consistent with increased heterogeneity/flexibility after activation. gp10 was modeled with full-length coverage in the structural model, reinforcing its status as a major ordered component of the wedge. (taylor2016structureofthe pages 6-8)
A focused interaction summary reports strong/robust gp10 interactions with gp11 and gp7, while not detecting strong direct pairwise interactions between gp10 and certain other wedge proteins (gp8, gp6, gp53, gp25) when assayed in isolation—consistent with assembly that proceeds via the gp7 backbone and multi-protein context-dependent interfaces. (arisaka2013proteininteractionsin pages 2-4)
In the T4 baseplate reconstruction, gp10 is located where it is clamped between the three “fingers” of gp11 and contacts the N-terminus of one gp12, placing it at a critical structural junction between the vertex protein network and short tail fibers. (kostyuchenko2003threedimensionalstructureof pages 2-3)
Direct new primary literature specifically on T4 gp10 in 2023–2024 was not retrieved in the current corpus; however, 2023–2024 high-resolution cryo-EM studies of other contractile-tailed phages provide important context for gp10-like wedge architectures and signal transduction principles.
A 2023 cryo-EM study of Vibrio phage XM1 emphasizes that its tail/baseplate uses fewer/smaller proteins and “depict[s] the minimum requirements for building an effective cell-envelope-penetr[at]ing machine.” Although it does not map XM1 proteins directly to T4 gp10 in the excerpt, it reinforces a conserved architectural principle: a central hub surrounded by six wedge modules. (wang2023structureofvibrio pages 1-3)
The same study quantifies interfaces involving a sheath initiator homologous to T4 gp25 (gp15 in XM1): gp15 forms large interfaces with sheath and wedge proteins (e.g., ~1642 Ų with sheath; ~1711 Ų with gp11; ~1615 Ų with the wedge core), and is proposed to act in transmitting signals from the baseplate to the sheath. This supports the broader modern view that baseplate conformational changes are coupled to sheath contraction through specific baseplate–sheath junction proteins, consistent with gp10’s placement in the T4 periphery-to-core signal path. (wang2023structureofvibrio pages 6-9)
Publication details: Wang et al., Viruses, 2023-07; https://doi.org/10.3390/v15081673. (wang2023structureofvibrio pages 1-3)
A 2024 cryo-EM structure of Anabaena myophage A-1(L) reports that “gp10” in that system forms 24 stacked rings of gp10 hexamers constituting the tail tube, not a baseplate wedge protein. This is a concrete example that reinforces the user’s warning: gp10 naming is not transferable across phages, and functional annotation must anchor on UniProt/organism context (T4 gp10 = baseplate wedge; other phages’ gp10 may be different). (yu2024structureofthe pages 2-4)
Publication details: Yu et al., Nature Communications, 2024-03; https://doi.org/10.1038/s41467-024-47006-z. (yu2024structureofthe pages 2-4)
A 2024 bioRxiv preprint on tail-fiber structural atlases reports “gp10-like C-terminal domains” used as modular elements in receptor-binding architectures, reinforcing that T4-like baseplate/tail modules are reused and recombined across phage diversity. While not direct functional evidence for T4 gp10, it supports the evolutionary interpretation that gp10-like folds function as reusable structural connectors in host-interaction machinery. (wang2023structureofvibrio pages 1-3)
Although gp10 itself is a structural protein (not a therapeutic enzyme), its mechanistic role in host attachment-to-injection coupling makes it relevant for phage engineering and for designing contractile injection systems as antibacterial platforms. Modern structural studies describe contractile injection systems (phage tails, pyocins, T6SS-like devices) as efficient envelope-penetrating nanomachines with potential antibacterial utility; by analogy, understanding wedge/baseplate proteins like gp10 informs rational modification of host recognition and infection efficiency. (wang2023structureofvibrio pages 1-3)
Across structural and biochemical work, the best-supported functional annotation for T4 gp10 (UniProt P10928) is:
| Aspect | Evidence summary | Key citations with DOI/URL and year |
|---|---|---|
| Identity/size/oligomerization | T4 gene product 10 (gp10; UniProt P10928) is a baseplate wedge protein of bacteriophage T4. It is 602 aa long and forms a trimer; structural studies place gp10 as a peripheral wedge/pin element in the baseplate. Crystal structures of the C-terminal fragment and cryo-EM fitting support a trimeric, elongated architecture about 210 Å long and ~60 Å in diameter. (yap2016roleofbacteriophage pages 1-3, leiman2006evolutionofbacteriophage pages 1-3, arisaka2016molecularassemblyand pages 1-2, kostyuchenko2003threedimensionalstructureof pages 2-3) | Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Leiman et al., 2006, J Mol Biol, doi:10.1016/j.jmb.2006.02.058, https://doi.org/10.1016/j.jmb.2006.02.058; Arisaka et al., 2016, Biophys Rev, doi:10.1007/s12551-016-0230-x, https://doi.org/10.1007/s12551-016-0230-x; Kostyuchenko et al., 2003, Nat Struct Biol, doi:10.1038/nsb970, https://doi.org/10.1038/nsb970 |
| Copy number | Reviews and structural summaries report gp10 stoichiometry as 18 copies per virion tail, corresponding to 3 copies per wedge in a six-wedge baseplate. Cryo-EM density/volume analysis is consistent with a gp10 trimer plus one gp7 per wedge region. (arisaka2016molecularassemblyand pages 2-4, arisaka2016molecularassemblyand pages 1-2, arisaka2013proteininteractionsin pages 2-4, kostyuchenko2003threedimensionalstructureof pages 2-3) | Arisaka et al., 2016, Biophys Rev, doi:10.1007/s12551-016-0230-x, https://doi.org/10.1007/s12551-016-0230-x; Arisaka & Kanamaru, 2013, Biophys Rev, doi:10.1007/s12551-013-0114-2, https://doi.org/10.1007/s12551-013-0114-2; Kostyuchenko et al., 2003, Nat Struct Biol, doi:10.1038/nsb970, https://doi.org/10.1038/nsb970 |
| Domain architecture | Gp10 is a four-domain trimeric protein. Domain I (residues 1–143) contains an N-terminal trimeric coiled coil (residues 1–39) and a prism/β-barrel region; domain II is a prism-like adaptor for short tail fibers gp12; domain III is a three-finger-like module providing the gp11 attachment site; domain IV (residues ~406–602) was crystallized and fitted into cryo-EM density. The domains have non-collinear threefold axes that reorient during baseplate rearrangement. Structural homology links gp10 to gp11 and gp12, and the N-terminus shows sequence similarity to gp9. (yap2016roleofbacteriophage pages 1-3, leiman2006evolutionofbacteriophage pages 3-5, leiman2006evolutionofbacteriophage pages 5-7, leiman2006evolutionofbacteriophage pages 1-3) | Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Leiman et al., 2006, J Mol Biol, doi:10.1016/j.jmb.2006.02.058, https://doi.org/10.1016/j.jmb.2006.02.058 |
| Key interaction partners | Experimentally supported interactions include strong binding to gp11 and gp7, followed by incorporation of gp8 and gp6 during wedge maturation. Domain II binds short tail fibers gp12; domain III provides the gp11 attachment site; domain IV contacts gp7 and, in the star state, gp9. In the 2003 baseplate reconstruction, gp10 sits clamped between gp11 fingers and contacts the N-terminus of one gp12. Protease protection shows gp10 becomes resistant when bound to gp7. (yap2016roleofbacteriophage pages 1-3, arisaka2013proteininteractionsin pages 2-4, yap2010sequentialassemblyof pages 3-5, leiman2006evolutionofbacteriophage pages 3-5, kostyuchenko2003threedimensionalstructureof pages 2-3) | Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Arisaka & Kanamaru, 2013, Biophys Rev, doi:10.1007/s12551-013-0114-2, https://doi.org/10.1007/s12551-013-0114-2; Yap et al., 2010, Macromol Biosci, doi:10.1002/mabi.201000042, https://doi.org/10.1002/mabi.201000042; Leiman et al., 2006, J Mol Biol, doi:10.1016/j.jmb.2006.02.058, https://doi.org/10.1016/j.jmb.2006.02.058; Kostyuchenko et al., 2003, Nat Struct Biol, doi:10.1038/nsb970, https://doi.org/10.1038/nsb970 |
| Role in wedge/baseplate assembly | Gp10 is an early wedge protein and part of the wedge initiation complex with gp11. Assembly proceeds sequentially through gp10–gp11, gp10–gp7, gp10–gp7–gp8, gp10–gp7–gp8–gp6, then gp53 and gp25. Reported sedimentation coefficients include gp11–gp10 9.7S, gp10–gp7 10.2S, gp10–gp7–gp8 12.1S, gp10–gp7–gp8–gp6 14.5S, gp10–gp7–gp8–gp6–gp53 15.0S, and gp10–gp7–gp8–gp6–gp53–gp25 15.3S; gp53 addition can drive assembly into a 43.7S star-shaped baseplate-like structure. The assembled T4 baseplate is a six-wedge, dome-like particle around a central hub; one early cryo-EM reconstruction measured the baseplate at ~520 Å diameter and ~270 Å long. (yap2010thebaseplatewedges pages 3-4, yap2010sequentialassemblyof pages 3-5, arisaka2016molecularassemblyand pages 2-4, arisaka2013proteininteractionsin pages 2-4, kostyuchenko2003threedimensionalstructureof pages 1-2) | Yap et al., 2010, J Mol Biol, doi:10.1016/j.jmb.2009.10.071, https://doi.org/10.1016/j.jmb.2009.10.071; Yap et al., 2010, Macromol Biosci, doi:10.1002/mabi.201000042, https://doi.org/10.1002/mabi.201000042; Arisaka & Kanamaru, 2013, Biophys Rev, doi:10.1007/s12551-013-0114-2, https://doi.org/10.1007/s12551-013-0114-2; Arisaka et al., 2016, Biophys Rev, doi:10.1007/s12551-016-0230-x, https://doi.org/10.1007/s12551-016-0230-x; Kostyuchenko et al., 2003, Nat Struct Biol, doi:10.1038/nsb970, https://doi.org/10.1038/nsb970 |
| Role in dome→star transition and sheath contraction triggering | Gp10 is not an enzyme; its primary function is structural and signaling-related within the baseplate. During the pre-attachment dome to post-attachment star transition, gp10 changes orientation and interaction partners. The whole gp10 rotates by ~100° about its long axis, and domain IV rotates by ~60°; gp10 loses interaction with gp12 and gains contact with gp9 while maintaining linkage to gp7. The gp7–gp10 covalent linkage is reported as important for maintaining baseplate structure during the conformational switch. The baseplate acts as the signaling center that transmits host-recognition information to trigger sheath contraction; gp10 is positioned at junctions connecting gp7, gp11, gp12, and gp9, so it participates in signal propagation rather than serving as the sole trigger. Cryo-EM captured pre- and post-attachment states at 4.11 Å and 6.77 Å; in vitro star-shaped wedge/baseplate maps reached 3.8 Å. (leiman2006evolutionofbacteriophage pages 1-3, yap2016roleofbacteriophage pages 1-3, leiman2006evolutionofbacteriophage pages 3-5, taylor2016structureofthe pages 1-3, taylor2016structureofthe pages 6-8, taylor2016structureofthe pages 3-6) | Leiman et al., 2006, J Mol Biol, doi:10.1016/j.jmb.2006.02.058, https://doi.org/10.1016/j.jmb.2006.02.058; Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Taylor et al., 2016, Nature, doi:10.1038/nature17971, https://doi.org/10.1038/nature17971 |
| Experimental methods/evidence types | Evidence comes from cryo-EM reconstructions of intact and in vitro-assembled baseplates, X-ray crystallography of gp10 fragments, fitting of atomic structures into cryo-EM maps, analytical ultracentrifugation/sedimentation velocity, gel filtration/SEC, His-tag pulldown and affinity isolation of assembly intermediates, SDS-PAGE, protease-sensitivity/protection assays, and comparative structural analysis. Key quantitative readouts include 3.8 Å cryo-EM for the in vitro assembled star-shaped baseplate-like complex, 4.11 Å and 6.77 Å for pre-/post-attachment baseplates, and multiple s-values for wedge intermediates. (yap2010thebaseplatewedges pages 3-4, yap2010sequentialassemblyof pages 3-5, yap2016roleofbacteriophage pages 1-3, taylor2016structureofthe pages 6-8) | Yap et al., 2010, J Mol Biol, doi:10.1016/j.jmb.2009.10.071, https://doi.org/10.1016/j.jmb.2009.10.071; Yap et al., 2010, Macromol Biosci, doi:10.1002/mabi.201000042, https://doi.org/10.1002/mabi.201000042; Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Taylor et al., 2016, Nature, doi:10.1038/nature17971, https://doi.org/10.1038/nature17971 |
| Functional annotation takeaway | The best-supported annotation for T4 gp10 is: trimeric baseplate wedge protein that nucleates and stabilizes wedge assembly with gp7/gp11, provides attachment interfaces for gp11 and short tail fibers gp12, contacts gp9 in the activated state, and contributes mechanically to the baseplate conformational switch that initiates downstream tail sheath contraction during infection. Its localization is extracellular, in the mature virion tail baseplate at the distal end of the phage particle. (yap2016roleofbacteriophage pages 1-3, arisaka2016molecularassemblyand pages 2-4, arisaka2016molecularassemblyand pages 1-2) | Yap et al., 2016, PNAS, doi:10.1073/pnas.1601654113, https://doi.org/10.1073/pnas.1601654113; Arisaka et al., 2016, Biophys Rev, doi:10.1007/s12551-016-0230-x, https://doi.org/10.1007/s12551-016-0230-x |
Table: This table summarizes the main functional-annotation evidence for bacteriophage T4 gp10 (UniProt P10928), including structure, stoichiometry, interaction partners, assembly pathway, and role in baseplate activation. It is useful as a compact evidence matrix linking specific mechanistic claims to the primary structural and biochemical literature.
References
(arisaka2016molecularassemblyand pages 1-2): Fumio Arisaka, Moh Lan Yap, Shuji Kanamaru, and Michael G. Rossmann. Molecular assembly and structure of the bacteriophage t4 tail. Biophysical Reviews, 8:385-396, Nov 2016. URL: https://doi.org/10.1007/s12551-016-0230-x, doi:10.1007/s12551-016-0230-x. This article has 55 citations and is from a peer-reviewed journal.
(leiman2006evolutionofbacteriophage pages 1-3): P.G. Leiman, M.M. Shneider, V.V. Mesyanzhinov, and M.G. Rossmann. Evolution of bacteriophage tails: structure of t4 gene product 10. Journal of molecular biology, 358 3:912-21, May 2006. URL: https://doi.org/10.1016/j.jmb.2006.02.058, doi:10.1016/j.jmb.2006.02.058. This article has 44 citations and is from a domain leading peer-reviewed journal.
(yap2016roleofbacteriophage pages 1-3): Moh Lan Yap, Thomas Klose, Fumio Arisaka, Jeffrey A. Speir, David Veesler, Andrei Fokine, and Michael G. Rossmann. Role of bacteriophage t4 baseplate in regulating assembly and infection. Proceedings of the National Academy of Sciences, 113:2654-2659, Feb 2016. URL: https://doi.org/10.1073/pnas.1601654113, doi:10.1073/pnas.1601654113. This article has 113 citations and is from a highest quality peer-reviewed journal.
(arisaka2016molecularassemblyand pages 2-4): Fumio Arisaka, Moh Lan Yap, Shuji Kanamaru, and Michael G. Rossmann. Molecular assembly and structure of the bacteriophage t4 tail. Biophysical Reviews, 8:385-396, Nov 2016. URL: https://doi.org/10.1007/s12551-016-0230-x, doi:10.1007/s12551-016-0230-x. This article has 55 citations and is from a peer-reviewed journal.
(kostyuchenko2003threedimensionalstructureof pages 2-3): Victor A Kostyuchenko, Petr G Leiman, Paul R Chipman, Shuji Kanamaru, Mark J van Raaij, Fumio Arisaka, Vadim V Mesyanzhinov, and Michael G Rossmann. Three-dimensional structure of bacteriophage t4 baseplate. Nature Structural Biology, 10:688-693, Sep 2003. URL: https://doi.org/10.1038/nsb970, doi:10.1038/nsb970. This article has 201 citations.
(leiman2006evolutionofbacteriophage pages 3-5): P.G. Leiman, M.M. Shneider, V.V. Mesyanzhinov, and M.G. Rossmann. Evolution of bacteriophage tails: structure of t4 gene product 10. Journal of molecular biology, 358 3:912-21, May 2006. URL: https://doi.org/10.1016/j.jmb.2006.02.058, doi:10.1016/j.jmb.2006.02.058. This article has 44 citations and is from a domain leading peer-reviewed journal.
(arisaka2013proteininteractionsin pages 2-4): Fumio Arisaka and Shuji Kanamaru. Protein interactions in the assembly of the tail of bacteriophage t4. Biophysical Reviews, 5:79-84, Apr 2013. URL: https://doi.org/10.1007/s12551-013-0114-2, doi:10.1007/s12551-013-0114-2. This article has 6 citations and is from a peer-reviewed journal.
(zhao2000stoichiometryandintersubunit pages 5-7): Li Zhao, Shigeki Takeda, Petr G. Leiman, and Fumio Arisaka. Stoichiometry and inter-subunit interaction of the wedge initiation complex, gp10-gp11, of bacteriophage t4. Biochimica et biophysica acta, 1479 1-2:286-92, Jun 2000. URL: https://doi.org/10.1016/s0167-4838(00)00015-7, doi:10.1016/s0167-4838(00)00015-7. This article has 19 citations.
(yap2010sequentialassemblyof pages 3-5): Moh Lan Yap, Kazuhiro Mio, Said Ali, Allen Minton, Shuji Kanamaru, and Fumio Arisaka. Sequential assembly of the wedge of the baseplate of phage t4 in the presence and absence of gp11 as monitored by analytical ultracentrifugation. Macromolecular bioscience, 10 7:808-13, Jul 2010. URL: https://doi.org/10.1002/mabi.201000042, doi:10.1002/mabi.201000042. This article has 13 citations and is from a peer-reviewed journal.
(taylor2016structureofthe pages 3-6): Nicholas M. I. Taylor, Nikolai S. Prokhorov, Ricardo C. Guerrero-Ferreira, Mikhail M. Shneider, Christopher Browning, Kenneth N. Goldie, Henning Stahlberg, and Petr G. Leiman. Structure of the t4 baseplate and its function in triggering sheath contraction. Nature, 533:346-352, May 2016. URL: https://doi.org/10.1038/nature17971, doi:10.1038/nature17971. This article has 355 citations and is from a highest quality peer-reviewed journal.
(taylor2016structureofthe pages 6-8): Nicholas M. I. Taylor, Nikolai S. Prokhorov, Ricardo C. Guerrero-Ferreira, Mikhail M. Shneider, Christopher Browning, Kenneth N. Goldie, Henning Stahlberg, and Petr G. Leiman. Structure of the t4 baseplate and its function in triggering sheath contraction. Nature, 533:346-352, May 2016. URL: https://doi.org/10.1038/nature17971, doi:10.1038/nature17971. This article has 355 citations and is from a highest quality peer-reviewed journal.
(wang2023structureofvibrio pages 1-3): Zhiqing Wang, Andrei Fokine, Xinwu Guo, Wen Jiang, Michael G. Rossmann, Richard J. Kuhn, Zhu-Hua Luo, and Thomas Klose. Structure of vibrio phage xm1, a simple contractile dna injection machine. Viruses, 15:1673, Jul 2023. URL: https://doi.org/10.3390/v15081673, doi:10.3390/v15081673. This article has 19 citations.
(wang2023structureofvibrio pages 6-9): Zhiqing Wang, Andrei Fokine, Xinwu Guo, Wen Jiang, Michael G. Rossmann, Richard J. Kuhn, Zhu-Hua Luo, and Thomas Klose. Structure of vibrio phage xm1, a simple contractile dna injection machine. Viruses, 15:1673, Jul 2023. URL: https://doi.org/10.3390/v15081673, doi:10.3390/v15081673. This article has 19 citations.
(yu2024structureofthe pages 2-4): Rong-Cheng Yu, Feng Yang, Hong-Yan Zhang, Pu Hou, Kang Du, Jie Zhu, Ning Cui, Xudong Xu, Yuxing Chen, Qiong Li, and Cong-Zhao Zhou. Structure of the intact tail machine of anabaena myophage a-1(l). Nature Communications, Mar 2024. URL: https://doi.org/10.1038/s41467-024-47006-z, doi:10.1038/s41467-024-47006-z. This article has 19 citations and is from a highest quality peer-reviewed journal.
(leiman2006evolutionofbacteriophage pages 5-7): P.G. Leiman, M.M. Shneider, V.V. Mesyanzhinov, and M.G. Rossmann. Evolution of bacteriophage tails: structure of t4 gene product 10. Journal of molecular biology, 358 3:912-21, May 2006. URL: https://doi.org/10.1016/j.jmb.2006.02.058, doi:10.1016/j.jmb.2006.02.058. This article has 44 citations and is from a domain leading peer-reviewed journal.
(yap2010thebaseplatewedges pages 3-4): Moh Lan Yap, Kazuhiro Mio, Petr G. Leiman, Shuji Kanamaru, and Fumio Arisaka. The baseplate wedges of bacteriophage t4 spontaneously assemble into hubless baseplate-like structure in vitro. Journal of molecular biology, 395 2:349-60, Jan 2010. URL: https://doi.org/10.1016/j.jmb.2009.10.071, doi:10.1016/j.jmb.2009.10.071. This article has 35 citations and is from a domain leading peer-reviewed journal.
(kostyuchenko2003threedimensionalstructureof pages 1-2): Victor A Kostyuchenko, Petr G Leiman, Paul R Chipman, Shuji Kanamaru, Mark J van Raaij, Fumio Arisaka, Vadim V Mesyanzhinov, and Michael G Rossmann. Three-dimensional structure of bacteriophage t4 baseplate. Nature Structural Biology, 10:688-693, Sep 2003. URL: https://doi.org/10.1038/nsb970, doi:10.1038/nsb970. This article has 201 citations.
(taylor2016structureofthe pages 1-3): Nicholas M. I. Taylor, Nikolai S. Prokhorov, Ricardo C. Guerrero-Ferreira, Mikhail M. Shneider, Christopher Browning, Kenneth N. Goldie, Henning Stahlberg, and Petr G. Leiman. Structure of the t4 baseplate and its function in triggering sheath contraction. Nature, 533:346-352, May 2016. URL: https://doi.org/10.1038/nature17971, doi:10.1038/nature17971. This article has 355 citations and is from a highest quality peer-reviewed journal.
id: P10928
gene_symbol: P10928
product_type: PROTEIN
status: INITIALIZED
taxon:
id: NCBITaxon:10665
label: Enterobacteria phage T4
description: 'TODO: Add description for P10928'
existing_annotations:
- term:
id: GO:0019076
label: viral release from host cell
evidence_type: IEA
original_reference_id: GO_REF:0000002
review:
summary: 'TODO: Review this GOA annotation'
action: PENDING
- term:
id: GO:0098003
label: viral tail assembly
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: 'TODO: Review this GOA annotation'
action: PENDING
- term:
id: GO:0098015
label: virus tail
evidence_type: IEA
original_reference_id: GO_REF:0000043
review:
summary: 'TODO: Review this GOA annotation'
action: PENDING
- term:
id: GO:0098025
label: virus tail, baseplate
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: 'TODO: Review this GOA annotation'
action: PENDING
- term:
id: GO:0098025
label: virus tail, baseplate
evidence_type: IDA
original_reference_id: PMID:27193680
review:
summary: 'TODO: Review this GOA annotation'
action: PENDING
references:
- id: GO_REF:0000002
title: Gene Ontology annotation through association of InterPro records with GO
terms
findings: []
- id: GO_REF:0000043
title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
findings: []
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods
findings: []
- id: PMID:27193680
title: Structure of the T4 baseplate and its function in triggering sheath contraction.
findings: []