Structural basis for the catalytic mechanism of phosphothreonine lyase

被引：36

作者：

Chen, Linjie ^{[1
,2
,3
]}

Wang, Huayi ^{[1
,2
,3
]}

Zhang, Jie ^{[1
]}

Gu, Lichuan ^{[4
]}

Huang, Niu ^{[1
,5
]}

Zhou, Jian-Min ^{[1
]}

Chai, Jijie ^{[1
]}

机构：

[1] Natl Inst Biol Sci, Beijing 102206, Peoples R China

[2] Beijing Union Med Coll, Beijing 100730, Peoples R China

[3] Grad Program Chinese Acad Med Sci, Beijing 100730, Peoples R China

[4] Shandong Univ, State Key Microbial Technol, Jinan 250100, Peoples R China

[5] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 01期

关键词：

D O I：

10.1038/nsmb1329

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：101 / 102

页数：2

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