1HJR

ATOMIC STRUCTURE OF THE RUVC RESOLVASE: A HOLLIDAY JUNCTION-SPECIFIC ENDONUCLEASE FROM E. COLI

Summary for 1HJR

• Entry DOI: 10.2210/pdb1hjr/pdb
• Descriptor: HOLLIDAY JUNCTION RESOLVASE (RUVC) (2 entities in total)
• Functional Keywords: site-specific recombinase
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 67970.41

Authors

Ariyoshi, M.,Vassylyev, D.G.,Morikawa, K. (deposition date: 1994-12-02, release date: 1995-02-07, Last modification date: 2024-02-07)

Primary citation

Ariyoshi, M.,Vassylyev, D.G.,Iwasaki, H.,Nakamura, H.,Shinagawa, H.,Morikawa, K.
Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli.
Cell(Cambridge,Mass.), 78:1063-1072, 1994

PubMed 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.

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)