Structural basis for the catalytic mechanism of phosphothreonine lyase
- 16 December 2007
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 15 (1) , 101-102
- https://doi.org/10.1038/nsmb1329
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.Keywords
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