3e4d | pdb_00003e4d

Structural and Kinetic Study of an S-Formylglutathione Hydrolase from Agrobacterium tumefaciens

spinqualitylabelsall models 3e4d, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e4d is a 6 chain structure with sequence from Agrobacterium fabrum str. C58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: CL, MG, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A9CJ11_AGRFC Serine hydrolase involved in the detoxification of formaldehyde.[RuleBase:RU363068] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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