1vsr
From Proteopedia
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'''VERY SHORT PATCH REPAIR (VSR) ENDONUCLEASE FROM ESCHERICHIA COLI''' | '''VERY SHORT PATCH REPAIR (VSR) ENDONUCLEASE FROM ESCHERICHIA COLI''' | ||
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[[Category: Nakagawa, M.]] | [[Category: Nakagawa, M.]] | ||
[[Category: Tsutakawa, S E.]] | [[Category: Tsutakawa, S E.]] | ||
| - | [[Category: | + | [[Category: Dna repair]] |
| - | [[Category: | + | [[Category: Endonuclease]] |
| - | [[Category: | + | [[Category: Mismatch recognition]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:52:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:52, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 12:52:42 2008
