Structural basis for the catalytic mechanism of phosphothreonine lyase
Structural basis for the catalytic mechanism of phosphothreonine lyase
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DOI：
10.1038/nsmb1329
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发表时间：
2008-01-01
影响因子：
16.8
通讯作者：
Chai, Jijie
中科院分区：
文献类型：
--
作者：
Chen, Linjie;Wang, Huayi;Chai, Jijie
沙门氏菌SpvC属于一个新的酶家族，命名为磷酸苏氨酸裂解酶，它不可逆转地失活有丝分裂原激活的蛋白激酶。本文报道的SpvC的晶体结构表明，底物多肽中的两个磷酸化残基主要介导SpvC对其的识别。底物诱导SpvC的构象变化在完全无溶剂的环境中隔离磷酸苏氨酸，防止磷酸基团的水解并促进消除反应。
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.