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• W2044967553 abstract "The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring." @default.
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• W2044967553 date "2009-06-01" @default.
• W2044967553 modified "2023-10-13" @default.
• W2044967553 title "The Structure of Gene Product 6 of Bacteriophage T4, the Hinge-Pin of the Baseplate" @default.
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• W2044967553 doi "https://doi.org/10.1016/j.str.2009.04.005" @default.
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