Journal
PROTEIN SCIENCE
Volume 18, Issue 10, Pages 2196-2202Publisher
WILEY
DOI: 10.1002/pro.216
Keywords
X-ray crystallography; hydrolase; protein structure; S-formylglutathione
Categories
Funding
- NSERC [RGPIN-250238]
- National Institutes of Health [GM62414]
- CIHR
- SHRF
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The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 angstrom 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.
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