The structure of a putative S-formylglutathione hydrolase from Agrobacterium tumefaciens.
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.
van Straaten
Karin E
KE
Department of Chemistry, University of Saskatchewan, Saskatoon, SK, Canada.
Gonzalez
Claudio F
CF
Valladares
Ricardo B
RB
Xu
Xiaohui
X
Savchenko
Alexei V
AV
Sanders
David A R
DA
D016960:Agrobacterium tumefaciens / Q000201:enzymology*; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D007700:Kinetics; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009154:Mutation / Q000235:genetics / Q000502:physiology; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013379:Substrate Specificity / Q000502:physiology; D013869:Thiolester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D050505:Mutant Proteins; D013869:Thiolester Hydrolases; C020149:s-formylglutathione hydrolase