3fz9

Crystal structure of poplar glutaredoxin S12 in complex with glutathione

spinqualitylabelsall models 3fz9, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fz9 is a 1 chain structure with sequence from Hybrid aspen. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GSH Related: 3fza Gene: GrxS12 (Hybrid aspen) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 Glutaredoxins (Grxs) are efficient catalysts for the reduction of mixed disulfides in glutathionylated proteins, using glutathione or thioredoxin reductases for their regeneration. Using GFP fusion, we have shown that poplar GrxS12, which possesses a monothiol (28)WCSYS(32) active site, is localized in chloroplasts. In the presence of reduced glutathione, the recombinant protein is able to reduce in vitro substrates, such as hydroxyethyldisulfide and dehydroascorbate, and to regenerate the glutathionylated glyceraldehyde-3-phosphate dehydrogenase. Although the protein possesses two conserved cysteines, it is functioning through a monothiol mechanism, the conserved C terminus cysteine (Cys(87)) being dispensable, since the C87S variant is fully active in all activity assays. Biochemical and crystallographic studies revealed that Cys(87) exhibits a certain reactivity, since its pK(a) is around 5.6. Coupled with thiol titration, fluorescence, and mass spectrometry analyses, the resolution of poplar GrxS12 x-ray crystal structure shows that the only oxidation state is a glutathionylated derivative of the active site cysteine (Cys(29)) and that the enzyme does not form inter- or intramolecular disulfides. Contrary to some plant Grxs, GrxS12 does not incorporate an iron-sulfur cluster in its wild-type form, but when the active site is mutated into YCSYS, it binds a [2Fe-2S] cluster, indicating that the single Trp residue prevents this incorporation. Structure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.,Couturier J, Koh CS, Zaffagnini M, Winger AM, Gualberto JM, Corbier C, Decottignies P, Jacquot JP, Lemaire SD, Didierjean C, Rouhier N J Biol Chem. 2009 Apr 3;284(14):9299-310. Epub 2009 Jan 21. PMID:19158074 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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