Gene Ontology annotation through association of InterPro records with GO terms.
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.
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Atomic structures of the bacteriophage T4 baseplate in pre- and post-attachment states define the architecture and conformational rotation of the gp10 peripheral wedge pin, its disulfide linkage to gp7, and its docking interfaces with gp11 and gp12.
"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."
Deep research summary for Bacteriophage T4 gene 10 (gp10)
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gp10 is a 602-residue homotrimer composed of four domains with non-collinear symmetry axes that rotate ~100 degrees overall (and ~60 degrees in domain IV) during the baseplate dome-to-star transition.
"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."
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During the hexagon-to-star baseplate transition, gp10 undergoes large-scale domain rotations to deploy the short tail fibers.
"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."
UniProtKB record for P10928 (10_BPT4)
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gp10 is a peripheral baseplate wedge protein involved in tail assembly that connects the short tail fibers to the baseplate and rotates as a lever during the dome-to-star transition.
"Peripheral baseplate protein that is part of the tail fiber network. Connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly."
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gp10 forms a disulfide-linked homotrimer where one subunit is disulfide-bonded to gp7 and the other two subunits are disulfide-bonded to each other, and interacts with gp11 and gp12.
"Homotrimer; disulfide-linked (PubMed:19896486, PubMed:27193680). Heteromultimer with gp7 (PubMed:19896486, PubMed:27193680); a gp10 molecule is disulfide-linked to gp7 and the other two remaining gp10 molecules form a disulfide bond (PubMed:27193680). The gp10 trimer interacts with gp11 trimer and with the short tail fiber (STF) composed of the gp12 trimer (PubMed:27193680)."