Brief Communication abstract
Nature Structural & Molecular Biology 15, 101 - 102 (2008)
Published online: 16 December 2007 | doi:10.1038/nsmb1329
Structural basis for the catalytic mechanism of phosphothreonine lyase
Linjie Chen1,2,5, Huayi Wang1,2,5, Jie Zhang2, Lichuan Gu3, Niu Huang2,4, Jian-Min Zhou2 & Jijie Chai2
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.
- Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.
- National Institute of Biological Sciences, Beijing 102206, China.
- State Key Lab of Microbial Technology, Shandong University, Jinan 250100, China.
- Department of Pharmaceutical Chemistry, University of California San Francisco, QB3 Building, 1700 Fourth Street, Box 2550, San Francisco, California 94143-2550, USA.
- These authors contributed equally to this work.
Correspondence to: Jijie Chai2 e-mail: chaijijie@nibs.ac.cn
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