Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.
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Yamada K, Kunishima N, Mayanagi K, Ohnishi T, Nishino T, Iwasaki H, Shinagawa H, Morikawa K
Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.
Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1442-7. Epub 2001 Feb 6.
- PubMed ID
- 11171970 [ View in PubMed]
- Abstract
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.