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The structure of a putative S‐formylglutathione hydrolase from Agrobacterium tumefaciens |
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| Authors: | Karin E van Straaten Claudio F Gonzalez Ricardo B Valladares Xiaohui Xu Alexei V Savchenko David A R Sanders |
| Institution: | 1. Department of Chemistry, University of Saskatchewan, Saskatoon, SK, Canada S7N 5C9;2. Ontario Center for Structural Proteomics, University Health Network, Toronto, Ontario, Canada M5G 2C4;3. Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32610‐3610 |
| Abstract: | The structure of the Atu1476 protein from Agrobacterium tumefaciens was determined at 2 Å 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 α/β 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. |
| Keywords: | X‐ray crystallography hydrolase protein structure S‐formylglutathione |