2Z8O

Structural basis for the catalytic mechanism of phosphothreonine lyase

2Z8O の概要

• エントリーDOI: 10.2210/pdb2z8o/pdb
• 関連するPDBエントリー: 2Z8M 2Z8N 2Z8P
• 分子名称: 27.5 kDa virulence protein, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: short three-helix bundle, distorted beta-strand sheet, lyase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56356.48

構造登録者

Chen, L.,Wang, H.,Gu, L.,Huang, N.,Zhou, J.M.,Chai, J. (登録日: 2007-09-07, 公開日: 2007-12-18, 最終更新日: 2024-11-20)

主引用文献

Chen, L.,Wang, H.,Zhang, J.,Gu, L.,Huang, N.,Zhou, J.M.,Chai, J.
Structural basis for the catalytic mechanism of phosphothreonine lyase.
Nat.Struct.Mol.Biol., 15:101-102, 2008

PubMed Abstract: Salmonella SpvC belongs to a new enzyme family designated phosphothreonine lyases that irreversibly inactivate mitogen-activated protein kinases. The crystal structure of SpvC reported here reveals that the two phosphorylated residues in the substrate peptide predominantly mediate its recognition by SpvC. Substrate-induced conformational changes in SpvC sequester the phosphothreonine in a completely solvent-free environment, preventing the hydrolysis of the phosphate group and facilitating the elimination reaction.

PubMed: 18084305
DOI: 10.1038/nsmb1329

実験手法

X-RAY DIFFRACTION (2.4 Å)