title: Structural similarities between Escherichia coli RuvA protein and other DNA-binding proteins and a mutational analysis of its binding to the holliday junction.
abstract: Comparison of the structure of Escherichia coli RuvA with other proteins in the Protein Data Bank gives insights into the probable modes of association of RuvA with the Holliday junction during homologous recombination. All three domains of the RuvA protein possess striking structural similarities to other DNA-binding proteins. Additionally, the second domain of RuvA contains two copies of the helix-hairpin-helix (HhH) structural motif, which has been implicated in non-sequence-specific DNA binding. The two copies of the motif are related by approximate 2-fold symmetry and may form a bidentate DNA-binding module. The results described provide support for the organization of the arms of the DNA in our RuvA/Holliday junction complex model and support the involvement of the HhH motifs in DNA binding.
authors.affiliation: Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, Western Bank, S10 2TN, UK.
authors.forename: J B
authors.initials: JB
authors.lastname: Rafferty
authors.forename: S M
authors.initials: SM
authors.lastname: Ingleston
authors.forename: D
authors.initials: D
authors.lastname: Hargreaves
authors.forename: P J
authors.initials: PJ
authors.lastname: Artymiuk
authors.forename: G J
authors.initials: GJ
authors.lastname: Sharples
authors.forename: R G
authors.initials: RG
authors.lastname: Lloyd
authors.forename: D W
authors.initials: DW
authors.lastname: Rice
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D004265:DNA Helicases; D019951:DNA Polymerase beta / Q000737:chemistry / Q000378:metabolism; D004269:DNA, Bacterial / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry* / Q000378:metabolism; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D019914:Taq Polymerase
chemical_list: D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D019914:Taq Polymerase; D019951:DNA Polymerase beta; C071059:Holliday junction DNA helicase, E coli; D004265:DNA Helicases