Crystallographic and functional studies of very short patch repair endonuclease

Susan E. Tsutakawa, Takanori Muto, Tomohiko Kawate, Hisato Jingami, Naoki Kunishima, Mariko Ariyoshi, Daisuke Kohda, Masako Nakagawa, Kosuke Morikawa

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)


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 Å 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.

Original languageEnglish
Pages (from-to)621-628
Number of pages8
JournalMolecular Cell
Issue number5
Publication statusPublished - 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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