1B63

MUTL COMPLEXED WITH ADPNP

1B63 の概要

• エントリーDOI: 10.2210/pdb1b63/pdb
• 分子名称: MUTL, MAGNESIUM ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: dna mismatch repair, atpase
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37869.99

構造登録者

Yang, W. (登録日: 1999-01-20, 公開日: 1999-06-08, 最終更新日: 2024-05-22)

主引用文献

Ban, C.,Junop, M.,Yang, W.
Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair.
Cell(Cambridge,Mass.), 97:85-97, 1999

PubMed Abstract: The MutL DNA mismatch repair protein has recently been shown to be an ATPase and to belong to an emerging ATPase superfamily that includes DNA topoisomerase II and Hsp90. We report here the crystal structures of a 40 kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate analog, ADPnP, and with product ADP. More than 60 residues that are disordered in the apoprotein structure become ordered and contribute to both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified by subsequent release of the gamma-phosphate, releases two key loops and leads to dissociation of the LN40 dimer. Dimerization of the LN40 region is required for and is the rate-limiting step in ATP hydrolysis by MutL. The ATPase activity of MutL is stimulated by DNA and likely acts as a switch to coordinate DNA mismatch repair.

PubMed: 10199405
DOI: 10.1016/S0092-8674(00)80717-5

実験手法

X-RAY DIFFRACTION (1.9 Å)