title: Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.
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.
authors.affiliation: Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Yamada
authors.forename: N
authors.initials: N
authors.lastname: Kunishima
authors.forename: K
authors.initials: K
authors.lastname: Mayanagi
authors.forename: T
authors.initials: T
authors.lastname: Ohnishi
authors.forename: T
authors.initials: T
authors.lastname: Nishino
authors.forename: H
authors.initials: H
authors.lastname: Iwasaki
authors.forename: H
authors.initials: H
authors.lastname: Shinagawa
authors.forename: K
authors.initials: K
authors.lastname: Morikawa
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009711:Nucleotides; D017433:Protein Structure, Secondary; D016963:Thermus thermophilus / Q000201:enzymology
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D009711:Nucleotides; C061260:RuvB protein, Bacteria; C071059:Holliday junction DNA helicase, E coli; D000251:Adenosine Triphosphatases; D004265:DNA Helicases