1X9Z

Crystal structure of the MutL C-terminal domain

1X9Z の概要

• エントリーDOI: 10.2210/pdb1x9z/pdb
• 関連するPDBエントリー: 1BKN 1NHI
• 分子名称: DNA mismatch repair protein mutL, CHLORIDE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: alpha-beta fold, dimer, replication, signaling protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41769.52

構造登録者

Guarne, A.,Ramon-Maiques, S.,Wolff, E.M.,Ghirlando, R.,Hu, X.,Miller, J.H.,Yang, W. (登録日: 2004-08-24, 公開日: 2004-10-26, 最終更新日: 2024-11-20)

主引用文献

Guarne, A.,Ramon-Maiques, S.,Wolff, E.M.,Ghirlando, R.,Hu, X.,Miller, J.H.,Yang, W.
Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair
Embo J., 23:4134-4145, 2004

PubMed Abstract: MutL assists the mismatch recognition protein MutS to initiate and coordinate mismatch repair in species ranging from bacteria to humans. The MutL N-terminal ATPase domain is highly conserved, but the C-terminal region shares little sequence similarity among MutL homologs. We report here the crystal structure of the Escherichia coli MutL C-terminal dimerization domain and the likelihood of its conservation among MutL homologs. A 100-residue proline-rich linker between the ATPase and dimerization domains, which generates a large central cavity in MutL dimers, tolerates sequence substitutions and deletions of one-third of its length with no functional consequences in vivo or in vitro. Along the surface of the central cavity, residues essential for DNA binding are located in both the N- and C-terminal domains. Each domain of MutL interacts with UvrD helicase and is required for activating the helicase activity. The DNA-binding capacity of MutL is correlated with the level of UvrD activation. A model of how MutL utilizes its ATPase and DNA-binding activities to mediate mismatch-dependent activation of MutH endonuclease and UvrD helicase is proposed.

PubMed: 15470502
DOI: 10.1038/sj.emboj.7600412

実験手法

X-RAY DIFFRACTION (2.1 Å)