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Cell. 1994 Sep 23;78(6):1063-72.

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

Author information

1
Protein Engineering Research Institute, Osaka, Japan.

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.

PMID:
7923356
DOI:
10.1016/0092-8674(94)90280-1
[Indexed for MEDLINE]

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