Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods
Structure of the T4 baseplate and its function in triggering sheath contraction.
-
Atomic cryo-EM reconstruction of the T4 baseplate in pre- and post-attachment states establishes the structure and triggering mechanism of the conserved baseplate wedge modules.
"Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail."
UniProtKB record for P19061 (BP07_BPT4)
-
gp7 is an intermediate and inner baseplate protein involved in viral tail assembly and, as part of the gp25-(gp6)2-gp7 module, in triggering sheath contraction.
"Intermediate/inner baseplate protein (PubMed:15315755, PubMed:27193680). The gp25-(gp6)2-gp7 module is involved in sheath contraction (PubMed:27193680). Involved in the tail assembly (PubMed:21129200)."
-
gp7 forms a (gp6)2-gp7 heterotrimer that interacts with gp25 and gp53, and is covalently linked via a disulfide bond to one monomer of the gp10 homotrimer.
"Heterotrimer with gp6; assembles as a (gp6)2-gp7 heterotrimeric molecule. The (gp6)2-gp7 heterotrimeric molecule further interacts with gp25 and gp53."
-
One subunit of the gp10 trimer forms an inter-protein disulfide bond with gp7.
"Heteromultimer with gp10; a gp10 molecule is disulfide-linked to gp7 and the other two remaining gp10 molecules form a disulfide bond."
Deep research report on bacteriophage T4 gene 7 (gp7; P19061)
-
gp7 serves as the structural backbone of each baseplate wedge, scaffolding other wedge subunits during assembly and transmitting the receptor-binding signal from the tail fibers to the inner baseplate.
"gp7 is a major **structural “backbone” protein** of a baseplate wedge. It (i) scaffolds/links other wedge proteins during assembly and (ii) participates in transmitting the host-binding signal from the tail fiber/receptor-binding network to the inner baseplate, enabling the conformational transition that triggers sheath contraction."
-
gp7 is covalently linked to gp10 via an inter-protein disulfide bond that maintains baseplate integrity during the dome-to-star conformational transition.
"gp7 is reported to be **covalently linked to gp10** via the only known inter-protein covalent bond in T4, and this linkage is implicated in maintaining the baseplate structure through the conformational switch."