title: Structural basis for the catalytic mechanism of phosphothreonine lyase.
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.
authors: Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.
authors: Linjie
authors: L
authors: Chen
authors: Huayi
authors: H
authors: Wang
authors: Jie
authors: J
authors: Zhang
authors: Lichuan
authors: L
authors: Gu
authors: Niu
authors: N
authors: Huang
authors: Jian-Min
authors: JM
authors: Zhou
authors: Jijie
authors: J
authors: Chai
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D019757:Carbon-Oxygen Lyases / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D008190:Lyases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010769:Phosphothreonine / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012475:Salmonella / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D010769:Phosphothreonine; D008190:Lyases; D019757:Carbon-Oxygen Lyases; C527194:phosphothreonine lyase, Salmonella enterica