Journal
STRUCTURE
Volume 20, Issue 8, Pages 1403-1413Publisher
CELL PRESS
DOI: 10.1016/j.str.2012.05.014
Keywords
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Funding
- NIH through a P41 program, National Center for Research Resources [RR17573]
- NIH [1R56 AI095974-01, 1R01GM100888-01A1]
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Packaging of viral genomes into empty procapsids is powered by a large DNA-packaging motor. In most viruses, this machine is composed of a large (L) and a small (S) terminase subunit complexed with a dodecamer of portal protein. Here we describe the 1.75 angstrom crystal structure of the bacteriophage P22 S-terminase in a nonameric conformation. The structure presents a central channel similar to 23 angstrom in diameter, sufficiently large to accommodate hydrated B-DNA. The last 23 residues of S-terminase are essential for binding to DNA and assembly to L-terminase. Upon binding to its own DNA, S-terminase functions as a specific activator of L-terminase ATPase activity. The DNA-dependent stimulation of ATPase activity thus rationalizes the exclusive specificity of genome-packaging motors for viral DNA in the crowd of host DNA, ensuring fidelity of packaging and avoiding wasteful ATP hydrolysis. This posits a model for DNA-dependent activation of genome-packaging motors of general interest in virology.
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