1VSR

VERY SHORT PATCH REPAIR (VSR) ENDONUCLEASE FROM ESCHERICHIA COLI

1VSR の概要

• エントリーDOI: 10.2210/pdb1vsr/pdb
• 分子名称: PROTEIN (VSR ENDONUCLEASE), ZINC ION (3 entities in total)
• 機能のキーワード: endonuclease, dna repair, mismatch recognition, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15850.43

構造登録者

Tsutakawa, S.E.,Muto, T.,Jingami, H.,Kunishima, N.,Ariyoshi, M.,Kohda, D.,Nakagawa, M.,Morikawa, K. (登録日: 1999-02-13, 公開日: 1999-10-27, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)