title: Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.
abstract: We present the X-ray structure of the RuvA-RuvB complex, which plays a crucial role in ATP-dependent branch migration. Two RuvA tetramers form the symmetric and closed octameric shell, where four RuvA domain IIIs spring out in the two opposite directions to be individually caught by a single RuvB. The binding of domain III deforms the protruding beta hairpin in the N-terminal domain of RuvB and thereby appears to induce a functional and less symmetric RuvB hexameric ring. The model of the RuvA-RuvB junction DNA ternary complex, constructed by fitting the X-ray structure into the averaged electron microscopic images of the RuvA-RuvB junction, appears to be more compatible with the branch migration mode of a fixed RuvA-RuvB interaction than with a rotational interaction mode.
authors.affiliation: Biomolecular Engineering Research Institute, Suita, Osaka, Japan.
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Yamada
authors.forename: Tomoko
authors.initials: T
authors.lastname: Miyata
authors.forename: Daisuke
authors.initials: D
authors.lastname: Tsuchiya
authors.forename: Takuji
authors.initials: T
authors.lastname: Oyama
authors.forename: Yoshie
authors.initials: Y
authors.lastname: Fujiwara
authors.forename: Takayuki
authors.initials: T
authors.lastname: Ohnishi
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Iwasaki
authors.forename: Hideo
authors.initials: H
authors.lastname: Shinagawa
authors.forename: Mariko
authors.initials: M
authors.lastname: Ariyoshi
authors.forename: Kouta
authors.initials: K
authors.lastname: Mayanagi
authors.forename: Kosuke
authors.initials: K
authors.lastname: Morikawa
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D004260:DNA Repair; D004261:DNA Replication; D004269:DNA, Bacterial / Q000737:chemistry / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D009097:Multienzyme Complexes; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D011995:Recombination, Genetic
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D020409:Molecular Motor Proteins; D009097:Multienzyme Complexes; D011993:Recombinant Fusion Proteins; C061260:RuvB protein, Bacteria; D000266:Adenylyl Imidodiphosphate; C071059:Holliday junction DNA helicase, E coli; D000251:Adenosine Triphosphatases; D004265:DNA Helicases