3ctf

Crystal structure of oxidized GRX2

spinqualitylabelsall models 3ctf, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ctf is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3ctg Gene: GRX2, TTR, TTR1, YDR513W, D9719.17 (ATCC 18824) Activity: Arsenate reductase (glutaredoxin), with EC number 1.20.4.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLRX2_YEAST] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. 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 glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor. Although sharing the same dithiolic CPYC active site and a sequence identity of 64%, they have been proved to play different roles during oxidative stress and to possess different glutathione-disulfide reductase activities. To address the structural basis of these differences, we solved the crystal structures of Grx2 in oxidized and reduced forms, at 2.10 A and 1.50 A, respectively. With the Grx1 structures we previously reported, comparative structural analyses revealed that Grx1 and Grx2 share a similar GSH binding site, except for a single residue substitution from Asp89 in Grx1 to Ser123 in Grx2. Site-directed mutagenesis in combination with activity assays further proved this single residue variation is critical for the different activities of yeast Grx1 and Grx2. Structural basis for the different activities of yeast Grx1 and Grx2.,Li WF, Yu J, Ma XX, Teng YB, Luo M, Tang YJ, Zhou CZ Biochim Biophys Acta. 2010 Jul;1804(7):1542-7. Epub 2010 Apr 24. PMID:20417731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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