ジャーナル: Structure / 年: 2009 タイトル: The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate. 著者: Anastasia A Aksyuk / Petr G Leiman / Mikhail M Shneider / Vadim V Mesyanzhinov / Michael G Rossmann / 要旨: 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 ...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.
A: Baseplate structural protein Gp6 B: Baseplate structural protein Gp6 C: Baseplate structural protein Gp6 D: Baseplate structural protein Gp6 E: Baseplate structural protein Gp6 F: Baseplate structural protein Gp6 G: Baseplate structural protein Gp6 H: Baseplate structural protein Gp6 I: Baseplate structural protein Gp6 J: Baseplate structural protein Gp6 K: Baseplate structural protein Gp6 L: Baseplate structural protein Gp6