3K0S

Crystal structure of E.coli DNA mismatch repair protein MutS, D693N mutant, in complex with GT mismatched DNA

3K0S の概要

• エントリーDOI: 10.2210/pdb3k0s/pdb
• 関連するPDBエントリー: 1E3M 1W7A
• 分子名称: DNA mismatch repair protein mutS, 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP*CP*CP*TP*AP*T)-3', 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP*GP*AP*C*AP*CP*T*GP*GP*TP*GP*CP*TP*TP*GP*GP*CP*AP*GP*CP*T)-3', ... (5 entities in total)
• 機能のキーワード: magnesium mutant, dna repair protein, protein-dna complex, atp-binding, dna damage, dna repair, dna-binding, nucleotide-binding, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 197836.41

構造登録者

Reumer, G.A.,Winterwerp, H.H.K.,Sixma, T.K. (登録日: 2009-09-25, 公開日: 2010-02-16, 最終更新日: 2023-09-06)

主引用文献

Lebbink, J.H.,Fish, A.,Reumer, A.,Natrajan, G.,Winterwerp, H.H.,Sixma, T.K.
Magnesium coordination controls the molecular switch function of DNA mismatch repair protein MutS.
J.Biol.Chem., 285:13131-13141, 2010

PubMed Abstract: The DNA mismatch repair protein MutS acts as a molecular switch. It toggles between ADP and ATP states and is regulated by mismatched DNA. This is analogous to G-protein switches and the regulation of their "on" and "off" states by guanine exchange factors. Although GDP release in monomeric GTPases is accelerated by guanine exchange factor-induced removal of magnesium from the catalytic site, we found that release of ADP from MutS is not influenced by the metal ion in this manner. Rather, ADP release is induced by the binding of mismatched DNA at the opposite end of the protein, a long-range allosteric response resembling the mechanism of activation of heterotrimeric GTPases. Magnesium influences switching in MutS by inducing faster and tighter ATP binding, allowing rapid downstream responses. MutS mutants with decreased affinity for the metal ion are impaired in fast switching and in vivo mismatch repair. Thus, the G-proteins and MutS conceptually employ the same efficient use of the high energy cofactor: slow hydrolysis in the absence of a signal and fast conversion to the active state when required.

PubMed: 20167596
DOI: 10.1074/jbc.M109.066001

実験手法

X-RAY DIFFRACTION (2.2 Å)