2ZQE

Crystal structure of the Smr domain of Thermus thermophilus MutS2

2ZQE の概要

• エントリーDOI: 10.2210/pdb2zqe/pdb
• 分子名称: MutS2 protein (2 entities in total)
• 機能のキーワード: alpha/beta, atp-binding, dna-binding, nucleotide-binding, dna binding protein
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8953.28

構造登録者

Fukui, K.,Kitamura, Y.,Nakagawa, N.,Masui, R.,Kuramitsu, S. (登録日: 2008-08-08, 公開日: 2008-09-30, 最終更新日: 2023-11-01)

主引用文献

Fukui, K.,Nakagawa, N.,Kitamura, Y.,Nishida, Y.,Masui, R.,Kuramitsu, S.
Crystal structure of MutS2 endonuclease domain and the mechanism of homologous recombination suppression
J.Biol.Chem., 283:33417-33427, 2008

PubMed Abstract: DNA recombination events need to be strictly regulated, because an increase in the recombinational frequency causes unfavorable alteration of genetic information. Recent studies revealed the existence of a novel anti-recombination enzyme, MutS2. However, the mechanism by which MutS2 inhibits homologous recombination has been unknown. Previously, we found that Thermus thermophilus MutS2 (ttMutS2) harbors an endonuclease activity and that this activity is confined to the C-terminal domain, whose amino acid sequence is widely conserved in a variety of proteins with unknown function from almost all organisms ranging from bacteria to man. In this study, we determined the crystal structure of the ttMutS2 endonuclease domain at 1.7-angstroms resolution, which resembles the structure of the DNase I-like catalytic domain of Escherichia coli RNase E, a sequence-nonspecific endonuclease. The N-terminal domain of ttMutS2, however, recognized branched DNA structures, including the Holliday junction and D-loop structure, a primary intermediate in homologous recombination. The full-length of ttMutS2 digested the branched DNA structures at the junction. These results indicate that ttMutS2 suppresses homologous recombination through a novel mechanism involving resolution of early intermediates.

PubMed: 18838375
DOI: 10.1074/jbc.M806755200

実験手法

X-RAY DIFFRACTION (1.7 Å)