Structural basis for the catalytic mechanism of phosphothreonine lyase

Nat Struct Mol Biol. 2008 Jan;15(1):101-2. doi: 10.1038/nsmb1329. Epub 2007 Dec 16.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Carbon-Oxygen Lyases / chemistry*
  • Carbon-Oxygen Lyases / metabolism*
  • Catalysis
  • Lyases / chemistry*
  • Lyases / metabolism*
  • Models, Molecular
  • Phosphothreonine / chemistry
  • Phosphothreonine / metabolism*
  • Protein Conformation
  • Salmonella / enzymology*

Substances

  • Bacterial Proteins
  • Phosphothreonine
  • Lyases
  • Carbon-Oxygen Lyases
  • phosphothreonine lyase, Salmonella enterica

Associated data

  • PDB/2Z8M
  • PDB/2Z8N
  • PDB/2Z8O
  • PDB/2Z8P