3vpq

Crystal structure of Bombyx mori sigma-class glutathione transferase in complex with glutathione

spinqualitylabelsall models 3vpq, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vpq is a 1 chain structure with sequence from Bombyx mori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.702Å Ligands: 1PE, GSH, PEG, PGO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5CCJ4_BOMMO Publication Abstract from PubMed BACKGROUND: Glutathione transferases (GSTs) are members of a major family of detoxification enzymes. Here, we report the crystal structure of a sigma-class GST of Bombyx mori, bmGSTS1, to gain insight into the mechanism catalysis. METHODS: The structure of bmGSTS1 and its complex with glutathione were determined at resolutions of 1.9A and 1.7A by synchrotron radiation and the molecular replacement method. RESULTS: The three-dimensional structure of bmGSTS1 shows that it exists as a dimer and is similar in structure to other GSTs with respect to its secondary and tertiary structures. Although striking similarities to the structure of prostaglandin D synthase were also detected, we were surprised to find that bmGSTS1 can convert prostaglandin H2 into its E2 form. Comparison of bmGSTS1 with its glutathione complex showed that bound glutathione was localized to the glutathione-binding site (G-site). Site-directed mutagenesis of bmGSTS1 mutants indicated that amino acid residues Tyr8, Leu14, Trp39, Lys43, Gln50, Met51, Gln63, and Ser64 in the G-site contribute to catalytic activity. CONCLUSION: We determined the tertiary structure of bmGSTS1 exhibiting prostaglandin E synthase activity. GENERAL SIGNIFICANCE: These results are, to our knowledge, the first report of a prostaglandin synthase activity in insects. Crystal structure of a Bombyx mori sigma-class glutathione transferase exhibiting prostaglandin E synthase activity.,Yamamoto K, Higashiura A, Suzuki M, Aritake K, Urade Y, Uodome N, Nakagawa A Biochim Biophys Acta. 2013 Jun;1830(6):3711-8. doi: 10.1016/j.bbagen.2013.02.021., Epub 2013 Mar 1. PMID:23458683 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione S-transferase 3D structures

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