Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli.
The crystal structure of the RuvC protein, a Holliday junction resolvase from E. coli, has been determined at 2.5 A 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 A 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.
Ariyoshi
M
M
Protein Engineering Research Institute, Osaka, Japan.
Vassylyev
D G
DG
Iwasaki
H
H
Nakamura
H
H
Shinagawa
H
H
Morikawa
K
K
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D001665:Binding Sites; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004269:DNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009713:Nucleotidyltransferases / Q000737:chemistry*; D011487:Protein Conformation; D011995:Recombination, Genetic; D016914:Ribonuclease H / Q000737:chemistry; D019895:Transposases
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D029968:Escherichia coli Proteins; C069806:ruvC protein, E coli; D009713:Nucleotidyltransferases; D019895:Transposases; D004706:Endodeoxyribonucleases; D016914:Ribonuclease H; C078856:ribonuclease HI