Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8

Kazuhiro Yamada, Naoki Kunishima, Kouta Mayanagi, Takayuki Ohnishi, Tatsuya Nishino, Hiroshi Iwasaki, Hideo Shinagawa, Kosuke Morikawa

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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 β-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.

Original languageEnglish
Pages (from-to)1442-1447
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number4
DOIs
Publication statusPublished - Feb 13 2001
Externally publishedYes

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