1hjr
From Proteopedia
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ATOMIC STRUCTURE OF THE RUVC RESOLVASE: A HOLLIDAY JUNCTION-SPECIFIC ENDONUCLEASE FROM E. COLI
Overview
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.
About this Structure
1HJR is a Single protein structure of sequence from Escherichia coli. Active as Crossover junction endodeoxyribonuclease, with EC number 3.1.22.4 Full crystallographic information is available from OCA.
Reference
Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli., Ariyoshi M, Vassylyev DG, Iwasaki H, Nakamura H, Shinagawa H, Morikawa K, Cell. 1994 Sep 23;78(6):1063-72. PMID:7923356
Page seeded by OCA on Thu Feb 21 13:01:59 2008
