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

M Ariyoshi; D G Vassylyev; H Iwasaki; H Nakamura; H Shinagawa; K Morikawa

doi:10.1016/0092-8674(94)90280-1

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

Cell. 1994 Sep 23;78(6):1063-72. doi: 10.1016/0092-8674(94)90280-1.

Authors

M Ariyoshi¹, D G Vassylyev, H Iwasaki, H Nakamura, H Shinagawa, K Morikawa

Affiliation

¹ Protein Engineering Research Institute, Osaka, Japan.

PMID: 7923356
DOI: 10.1016/0092-8674(94)90280-1

Abstract

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.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Bacterial Proteins / chemistry*
Base Sequence
Binding Sites
Computer Simulation
Crystallography, X-Ray
DNA, Bacterial / chemistry
DNA, Bacterial / metabolism
Endodeoxyribonucleases / chemistry*
Escherichia coli / enzymology*
Escherichia coli Proteins*
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
Nucleotidyltransferases / chemistry*
Protein Conformation
Recombination, Genetic
Ribonuclease H / chemistry
Transposases

Substances

Bacterial Proteins
DNA, Bacterial
Escherichia coli Proteins
ruvC protein, E coli
Nucleotidyltransferases
Transposases
Endodeoxyribonucleases
Ribonuclease H
ribonuclease HI