Atomic structure of the RuvC resolvase: A holliday junction-specific endonuclease from E. coli

Academic Article

Abstract

  • The crystal structure of the RuvC protein, a Holliday junction resolvase from E. coli, has been determined at 2.5 Å resolution. The enzyme forms a dimer of 19 kDa subunits related by a dyad axis. Together with results from extensive mutational analyses, the refined structure reveals that the catalytic center, comprising four acidic residues, lies at the bottom of a cleft that nicely fits a DNA duplex. The structural features of the dimer, with a 30 Å spacing between the two catalytic centers, provide a substantially defined image of the Holliday junction architecture. The folding topology in the vicinity of the catalytic site exhibits a striking similarity to that of RNAase H1 from E. coli. © 1994.
  • Published In

  • Cell  Journal
  • Digital Object Identifier (doi)

    Author List

  • Ariyoshi M; Vassylyev DG; Iwasaki H; Nakamura H; Shinagawa H; Morikawa K
  • Start Page

  • 1063
  • End Page

  • 1072
  • Volume

  • 78
  • Issue

  • 6