Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Structure of the T4 baseplate and its function in triggering sheath contraction.
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Atomic cryo-EM reconstruction of the T4 baseplate resolves the structure and interactions of the baseplate wedge proteins in pre- and post-attachment states.
"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 P19062 (BP08_BPT4)
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gp8 is an intermediate baseplate protein involved in viral tail assembly.
"Intermediate baseplate protein. Involved in the tail assembly."
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gp8 forms a homodimer that interacts with gp7 and is present in 12 copies per baseplate.
"Homodimer (PubMed:19896486, PubMed:2403438, PubMed:27193680). Interacts with gp7."
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Twelve copies of gp8 are present in the assembled baseplate.
"Note=Present in 12 copies in the baseplate."
Deep research report on bacteriophage T4 gene 8 (gp8; P19062)
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gp8 stabilizes the baseplate wedge by binding a stretched linker of gp7, reducing its flexibility so that gp6 can bind productively to complete wedge assembly.
"A central mechanistic insight is that gp8 acts as a stabilizing wedge component by binding a gp7 linker that is stretched upon earlier assembly steps, thereby reducing gp7 flexibility and allowing gp6 to bind in a productive orientation to complete wedge assembly."
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gp8 must bind to the gp10-gp7 complex before gp6 can attach and fold into the wedge.
"gp8 is required before gp6 can attach to the wedge, and gp8 has been described as essential for gp6 folding in this assembly context."