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.
journal_name
Proc Natl Acad Sci U S Aauthors
Yamada K,Kunishima N,Mayanagi K,Ohnishi T,Nishino T,Iwasaki H,Shinagawa H,Morikawa Kdoi
10.1073/pnas.031470598keywords:
subject
Has Abstractpub_date
2001-02-13 00:00:00pages
1442-7issue
4eissn
0027-8424issn
1091-6490pii
031470598journal_volume
98pub_type
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