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3ctf

From Proteopedia

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{{Seed}}
 
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[[Image:3ctf.png|left|200px]]
 
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==Crystal structure of oxidized GRX2==
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The line below this paragraph, containing "STRUCTURE_3ctf", creates the "Structure Box" on the page.
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<StructureSection load='3ctf' size='340' side='right'caption='[[3ctf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ctf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CTF FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ctf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctf OCA], [https://pdbe.org/3ctf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ctf RCSB], [https://www.ebi.ac.uk/pdbsum/3ctf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ctf ProSAT]</span></td></tr>
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{{STRUCTURE_3ctf| PDB=3ctf | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLRX2_YEAST 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.<ref>PMID:9571241</ref> <ref>PMID:11875065</ref> <ref>PMID:12684511</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/3ctf_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ctf ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of oxidized GRX2===
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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<ref>PMID:20417731</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20417731}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3ctf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20417731 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20417731}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3CTF is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CTF OCA].
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==Reference==
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<ref group="xtra">PMID:20417731</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Teng, Y B.]]
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[[Category: Teng YB]]
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[[Category: Yu, J.]]
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[[Category: Yu J]]
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[[Category: Zhou, C Z.]]
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[[Category: Zhou CZ]]
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[[Category: Electron transport]]
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[[Category: Mitochondrion]]
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[[Category: Oxidized form]]
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[[Category: Oxidoreductase]]
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[[Category: Redox-active center]]
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[[Category: Transit peptide]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 1 09:26:05 2010''
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Current revision

Crystal structure of oxidized GRX2

PDB ID 3ctf

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