2hqm | pdb_00002hqm

Crystal Structure of Glutathione Reductase Glr1 from the Yeast Saccharomyces cerevisiae

spinqualitylabelsall models 2hqm, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hqm is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, GOL, GSH, NAG, PO4 Activity: Glutathione-disulfide reductase, with EC number 1.8.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GSHR_YEAST] Maintains high levels of reduced glutathione in the cytosol. 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 Yeast glutathione (GSH) reductase Glr1 is a dimeric flavo-oxidoreductase involved in cytoplasmic and mitochondrial redox regulatory systems. It reduces the oxidized GSH GSSG to the reduced form, GSH with NADPH as electron donor and FAD as coenzyme. Crystal structures and enzymatic mechanisms of GSH reductases from Escherichia coli and Homo sapiens have been well investigated, whereas the structural properties of yeast Glr1 remain unknown. Herein, we overexpressed Saccharomyces cerevisiae Glr1 in Pichia pastoris GS115 and determined its crystal structure at 2.40 A resolution. Although the overall structure and the active site are much conserved, obvious variety was found at the interface of Glr1 monomers when superimposed against the homolog from E. coli or human. The nonconserved C239 is exposed to the solvent and accessible to GSH or GSSG enriched in a microenvironment around the Glr1 molecules, leading to the partial and transient glutathionylation, as primarily identified from the 2Fo-Fc electron density map and further confirmed by biochemical assays. Meanwhile N278 at the vicinity of NADP-binding pocket was artificially glycosylated when heterogeneously overexpressed in P. pastoris. The highly motile oligosaccharide chain linked to N278 of the recombinant Glr1 interferes with the entry of NADPH, which results in a dramatic increase of Km for NAPDH and a significant decrease of turnover number, when compared with the native protein. Crystal structure of glutathione reductase Glr1 from the yeast Saccharomyces cerevisiae.,Yu J, Zhou CZ Proteins. 2007 Sep 1;68(4):972-9. PMID:17554778 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glutathione Reductase

Proteopedia Page Contributors and Editors (what is this?)

OCA