Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 towards short to medium chain esters, unlike the other known SFGHs which have greater affinity towards shorter chained esters. A potential role for Cys54 in regulation of enzyme activity through S-glutathionylation is also proposed.
The structure of a putative S-formylglutathione hydrolase from agrobacterium tumefaciens.,van Straaten KE, Gonzalez CF, Valladares RB, Xu X, Savchenko AV, Sanders DA Protein Sci. 2009 Aug 3. PMID:19653299[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Straaten KE, Gonzalez CF, Valladares RB, Xu X, Savchenko AV, Sanders DA. The structure of a putative S-formylglutathione hydrolase from agrobacterium tumefaciens. Protein Sci. 2009 Aug 3. PMID:19653299 doi:10.1002/pro.216
