1vsr

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1vsr, resolution 1.8Å

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VERY SHORT PATCH REPAIR (VSR) ENDONUCLEASE FROM ESCHERICHIA COLI

Overview

Vsr endonuclease plays a crucial role in the repair of TG mismatched base, pairs, which are generated by the spontaneous degradation of methylated, cytidines; Vsr recognizes the mismatched base pair and cleaves the, phosphate backbone 5' to the thymidine. We have determined the crystal, structure of a truncated form of this endonuclease at 1.8 A resolution., The protein contains one structural zinc-binding module. Unexpectedly, its, overall topology resembles members of the type II restriction endonuclease, family. Subsequent mutational and biochemical analyses showed that certain, elements in the catalytic site are also conserved. However, the, identification of a critical histidine and evidence of an active site, metal-binding coordination that is novel to endonucleases indicate a, distinct catalytic mechanism.

About this Structure

1VSR is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Crystallographic and functional studies of very short patch repair endonuclease., Tsutakawa SE, Muto T, Kawate T, Jingami H, Kunishima N, Ariyoshi M, Kohda D, Nakagawa M, Morikawa K, Mol Cell. 1999 May;3(5):621-8. PMID:10360178

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