3rhc | pdb_00003rhc

Crystal structure of the holo form of glutaredoxin C5 from Arabidopsis thaliana

spinqualitylabelsall models 3rhc, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rhc is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FES, GSH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GRXC5_ARATH Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin. Publication Abstract from PubMed Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides i.e. protein-glutathione adducts, and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, is shown to be localized in chloroplasts. A comparison of the biochemical, structural and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicates that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the X-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys32) is required for cluster formation. In addition, thiol titrations, fluorescence measurements and mass spectrometry analyses show that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism. Arabidopsis chloroplastic glutaredoxin C5 as a model to explore the molecular determinants for iron-sulfur cluster binding into glutaredoxins.,Couturier J, Stroher E, Albetel AN, Roret T, Muthuramalingam M, Tarrago L, Seidel T, Tsan P, Jacquot JP, Johnson MK, Dietz KJ, Didierjean C, Rouhier N J Biol Chem. 2011 Jun 1. PMID:21632542 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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