Structural basis for the catalytic mechanism of phosphothreonine lyase.
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.
Chen
Linjie
L
Graduate Program in Chinese Academy of Medical Sciences and Beijing Union Medical College, Beijing 100730, China.
Wang
Huayi
H
Zhang
Jie
J
Gu
Lichuan
L
Huang
Niu
N
Zhou
Jian-Min
JM
Chai
Jijie
J
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*
D001426:Bacterial Proteins; D010769:Phosphothreonine; D008190:Lyases; D019757:Carbon-Oxygen Lyases; C527194:phosphothreonine lyase, Salmonella enterica