TY - JOUR
T1 - The Structure of Gene Product 6 of Bacteriophage T4, the Hinge-Pin of the Baseplate
AU - Aksyuk, Anastasia A.
AU - Leiman, Petr G.
AU - Shneider, Mikhail M.
AU - Mesyanzhinov, Vadim V.
AU - Rossmann, Michael G.
N1 - Funding Information:
We thank Victor Kostyuchenko, Siyang Sun, Ye Xiang, Andrei Fokine, and Anthony Battisti for helpful discussions. We thank Carol Greski and Sheryl Kelly for help in the preparation of the manuscript. We thank the staff of beamline 23 (GM/CA) of the Advanced Photon Source for excellent support of our data collection. We also thank “CCP4 School: From Data Processing to Structure Refinement and Beyond,” held in May 2008 at Argonne National Laboratory, for helpful discussions of refinement strategies and Pavel Afonine for advice on the use of the PHENIX.REFINE program. This work was supported by a National Science Foundation grant (MCB-0443899, to M.G.R.) and a Purdue Research Foundation grant (to M.G.R. in support of A.A.A.).
PY - 2009/6/10
Y1 - 2009/6/10
N2 - 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 ∼15°, accounting for a 10 Å radial increase in the diameter of the gp6 ring.
AB - 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 ∼15°, accounting for a 10 Å radial increase in the diameter of the gp6 ring.
KW - PROTEINS
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U2 - 10.1016/j.str.2009.04.005
DO - 10.1016/j.str.2009.04.005
M3 - Article
C2 - 19523898
AN - SCOPUS:66749084492
SN - 0969-2126
VL - 17
SP - 800
EP - 808
JO - Structure
JF - Structure
IS - 6
ER -