PMID:7923356

Citation	Ariyoshi, M, Vassylyev, DG, Iwasaki, H, Nakamura, H, Shinagawa, H and Morikawa, K (1994) Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli. Cell 78:1063-72
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.
Links	PubMed
Keywords	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
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