The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens

Protein Sci. 2009 Oct;18(10):2196-202. doi: 10.1002/pro.216.

Abstract

The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 A resolution. The crystal structure and biochemical characterization of this enzyme support the conclusion that this protein is an S-formylglutathione hydrolase (AtuSFGH). The three-dimensional structure of AtuSFGH contains the alpha/beta hydrolase fold topology and exists as a homo-dimer. Contacts between the two monomers in the dimer are formed both by hydrogen bonds and salt bridges. Biochemical characterization reveals that AtuSFGH hydrolyzes C--O bonds with high affinity toward short to medium chain esters, unlike the other known SFGHs which have greater affinity toward shorter chained esters. A potential role for Cys54 in regulation of enzyme activity through S-glutathionylation is also proposed.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agrobacterium tumefaciens / enzymology*
  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Kinetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutant Proteins / chemistry*
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Mutation / genetics
  • Mutation / physiology
  • Protein Folding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Substrate Specificity / physiology
  • Thiolester Hydrolases / chemistry*
  • Thiolester Hydrolases / genetics
  • Thiolester Hydrolases / metabolism

Substances

  • Mutant Proteins
  • Thiolester Hydrolases
  • s-formylglutathione hydrolase