1vsr
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(New page: 200px<br /><applet load="1vsr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vsr, resolution 1.8Å" /> '''VERY SHORT PATCH REPA...)
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Revision as of 03:00, 21 November 2007
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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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