Structural basis for the catalytic mechanism of phosphothreonine lyase.

Linjie Chen, Huayi Wang, Jie Zhang, Lichuan Gu, Niu Huang, Jian-Min Zhou, Jijie Chai

Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.

Nature structural & molecular biology 2008 Jan

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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.

Citation

Linjie Chen, Huayi Wang, Jie Zhang, Lichuan Gu, Niu Huang, Jian-Min Zhou, Jijie Chai. Structural basis for the catalytic mechanism of phosphothreonine lyase. Nature structural & molecular biology. 2008 Jan;15(1):101-2