1hqc
From Proteopedia
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STRUCTURE OF RUVB FROM THERMUS THERMOPHILUS HB8
Overview
We report here the crystal structure of the RuvB motor protein from, Thermus thermophilus HB8, which drives branch migration of the Holliday, junction during homologous recombination. RuvB has a crescent-like, architecture consisting of three consecutive domains, the first two of, which are involved in ATP binding and hydrolysis. DNA is likely to, interact with a large basic cleft, which encompasses the ATP-binding, pocket and domain boundaries, whereas the junction-recognition protein, RuvA may bind a flexible beta-hairpin protruding from the N-terminal, domain. The structures of two subunits, related by a noncrystallographic, pseudo-2-fold axis, imply that conformational changes of motor protein, coupled with ATP hydrolysis may reflect motility essential for its, translocation around double-stranded DNA.
About this Structure
1HQC is a Single protein structure of sequence from Thermus thermophilus with MG and ADE as ligands. Active as Adenosinetriphosphatase, with EC number 3.6.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8., Yamada K, Kunishima N, Mayanagi K, Ohnishi T, Nishino T, Iwasaki H, Shinagawa H, Morikawa K, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1442-7. Epub 2001 Feb 6. PMID:11171970
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