4lmv

Crystal structure of glutathione transferase GSTFuA2 from Phanerochaete chrysosporium

spinqualitylabelsall models 4lmv, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lmv is a 6 chain structure with sequence from Chrysosporium pruinosum (gilman & abbott) carmich.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, FLC Related: 4g19, 4f03 Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Glutathione transferases (GSTs) form a superfamily of multifunctional proteins with essential roles in cellular detoxification processes and endogenous metabolism. The distribution of fungal-specific class A GSTs was investigated in saprotrophic fungi revealing a recent diversification within this class. Biochemical characterization of eight GSTFuA isoforms from Phanerochaete chrysosporium and Coprinus cinereus demonstrated functional diversity in saprotrophic fungi. The three-dimensional structures of three P. chrysosporium isoforms feature structural differences explaining the functional diversity of these enzymes. Competition experiments between fluorescent probes, and various molecules, showed that these GSTs function as ligandins with various small aromatic compounds, derived from lignin degradation or not, at a L-site overlapping the glutathione binding pocket. By combining genomic data with structural and biochemical determinations, we propose that this class of GST has evolved in response to environmental constraints induced by wood chemistry. Diversification of fungal specific class a glutathione transferases in saprotrophic fungi.,Mathieu Y, Prosper P, Favier F, Harvengt L, Didierjean C, Jacquot JP, Morel-Rouhier M, Gelhaye E PLoS One. 2013 Nov 20;8(11):e80298. doi: 10.1371/journal.pone.0080298., eCollection 2013. PMID:24278272 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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