1VSR

VERY SHORT PATCH REPAIR (VSR) ENDONUCLEASE FROM ESCHERICHIA COLI

Summary for 1VSR

• Entry DOI: 10.2210/pdb1vsr/pdb
• Descriptor: PROTEIN (VSR ENDONUCLEASE), ZINC ION (3 entities in total)
• Functional Keywords: endonuclease, dna repair, mismatch recognition, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 15850.43

Authors

Tsutakawa, S.E.,Muto, T.,Jingami, H.,Kunishima, N.,Ariyoshi, M.,Kohda, D.,Nakagawa, M.,Morikawa, K. (deposition date: 1999-02-13, release date: 1999-10-27, Last modification date: 2023-12-27)

Primary citation

Tsutakawa, S.E.,Muto, T.,Kawate, T.,Jingami, H.,Kunishima, N.,Ariyoshi, M.,Kohda, D.,Nakagawa, M.,Morikawa, K.
Crystallographic and functional studies of very short patch repair endonuclease.
Mol.Cell, 3:621-628, 1999

PubMed Abstract: 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.

PubMed: 10360178
DOI: 10.1016/S1097-2765(00)80355-X

Experimental method

X-RAY DIFFRACTION (1.8 Å)