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Title
Japanese: 
English:Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8 
Author
Japanese: Yamada, K., Kunishima, N., Mayanagi, K., Ohnishi, T., Nishino, T., 岩崎博史, Shinagawa, H., Morikawa, K..  
English: Yamada, K., Kunishima, N., Mayanagi, K., Ohnishi, T., Nishino, T., Hiroshi Iwasaki, Shinagawa, H., Morikawa, K..  
Language English 
Journal/Book name
Japanese:Proceedings of the National Academy of Sciences of the United States of America 
English:Proceedings of the National Academy of Sciences of the United States of America 
Volume, Number, Page Vol. 98    No. 4    pp. 1442-1447
Published date Feb. 2001 
Publisher
Japanese: 
English: 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
Official URL http://www.scopus.com/inward/record.url?eid=2-s2.0-0035852703&partnerID=MN8TOARS
 
DOI https://doi.org/10.1073/pnas.98.4.1442
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.

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