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Structure and mechanism of the ATPase that powers viral genome packaging.

Proc Natl Acad Sci U S A. 2015; 
Hilbert BJ, Hayes JA, Stone NP, Duffy CM, Sankaran B, Kelch BA.
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摘要

Many viruses package their genomes into procapsids using an ATPase machine that is among the most powerful known biological motors. However, how this motor couples ATP hydrolysis to DNA translocation is still unknown. Here, we introduce a model system with unique properties for studying motor structure and mechanism. We describe crystal structures of the packaging motor ATPase domain that exhibit nucleotide-dependent conformational changes involving a large rotation of an entire subdomain. We also identify the arginine finger residue that catalyzes ATP hydrolysis in a neighboring motor subunit, illustrating that previous models for motor structure need revision. Our findings allow us to derive a structural mode... More

关键词

ASCE ATPase; bacteriophage; motor protein; thermophile; translocase