3KDG

C-terminal domain of Bacillus subtilis MutL crystal form II

3KDG の概要

• エントリーDOI: 10.2210/pdb3kdg/pdb
• 関連するPDBエントリー: 3GAB 3KDK
• 分子名称: DNA mismatch repair protein mutL (2 entities in total)
• 機能のキーワード: mismatch repair, mutl, endonuclease, dna damage, dna repair, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 45734.45

構造登録者

Guarne, A.,Pillon, M.C. (登録日: 2009-10-22, 公開日: 2010-07-21, 最終更新日: 2023-09-06)

主引用文献

Pillon, M.C.,Lorenowicz, J.J.,Uckelmann, M.,Klocko, A.D.,Mitchell, R.R.,Chung, Y.S.,Modrich, P.,Walker, G.C.,Simmons, L.A.,Friedhoff, P.,Guarne, A.
Structure of the endonuclease domain of MutL: unlicensed to cut.
Mol.Cell, 39:145-151, 2010

PubMed Abstract: DNA mismatch repair corrects errors that have escaped polymerase proofreading, increasing replication fidelity 100- to 1000-fold in organisms ranging from bacteria to humans. The MutL protein plays a central role in mismatch repair by coordinating multiple protein-protein interactions that signal strand removal upon mismatch recognition by MutS. Here we report the crystal structure of the endonuclease domain of Bacillus subtilis MutL. The structure is organized in dimerization and regulatory subdomains connected by a helical lever spanning the conserved endonuclease motif. Additional conserved motifs cluster around the lever and define a Zn(2+)-binding site that is critical for MutL function in vivo. The structure unveils a powerful inhibitory mechanism to prevent undesired nicking of newly replicated DNA and allows us to propose a model describing how the interaction with MutS and the processivity clamp could license the endonuclease activity of MutL. The structure also provides a molecular framework to propose and test additional roles of MutL in mismatch repair.

PubMed: 20603082
DOI: 10.1016/j.molcel.2010.06.027

実験手法

X-RAY DIFFRACTION (2 Å)