1BKN

CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL

1BKN の概要

• エントリーDOI: 10.2210/pdb1bkn/pdb
• 分子名称: MUTL (2 entities in total)
• 機能のキーワード: dna repair, atpase, dna binding
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78599.20

構造登録者

Yang, W.,Ban, C. (登録日: 1998-07-09, 公開日: 1999-05-11, 最終更新日: 2024-02-07)

主引用文献

Ban, C.,Yang, W.
Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis.
Cell(Cambridge,Mass.), 95:541-552, 1998

PubMed Abstract: MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.

PubMed: 9827806
DOI: 10.1016/S0092-8674(00)81621-9

実験手法

X-RAY DIFFRACTION (2.9 Å)