Journal
STRUCTURE
Volume 17, Issue 6, Pages 800-808Publisher
CELL PRESS
DOI: 10.1016/j.str.2009.04.005
Keywords
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Funding
- National Science Foundation [MCB-0443899]
- Purdue Research Foundation
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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 similar to 15 degrees, accounting for a 10 angstrom radial increase in the diameter of the gp6 ring.
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