1JHC

LEXA S119A C-TERMINAL TRYPTIC FRAGMENT

1JHC の概要

• エントリーDOI: 10.2210/pdb1jhc/pdb
• 関連するPDBエントリー: 1JHE 1JHF 1JHH
• 分子名称: LEXA REPRESSOR (2 entities in total)
• 機能のキーワード: lexa sos repressor, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15178.40

構造登録者

Luo, Y.,Pfuetzner, R.A.,Mosimann, S.,Little, J.W.,Strynadka, N.C.J. (登録日: 2001-06-27, 公開日: 2001-09-19, 最終更新日: 2023-08-16)

主引用文献

Luo, Y.,Pfuetzner, R.A.,Mosimann, S.,Paetzel, M.,Frey, E.A.,Cherney, M.,Kim, B.,Little, J.W.,Strynadka, N.C.
Crystal structure of LexA: a conformational switch for regulation of self-cleavage.
Cell(Cambridge,Mass.), 106:585-594, 2001

PubMed Abstract: LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the catalytic center. Our analysis provides insight into the structural and energetic features that modulate the interconversion between these two forms and hence the rate of the self-cleavage reaction. We suggest RecA activates the self-cleavage of LexA and related proteins through selective stabilization of the cleavable conformation.

PubMed: 11551506
DOI: 10.1016/S0092-8674(01)00479-2

実験手法

X-RAY DIFFRACTION (2 Å)