3ctf: Difference between revisions

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{{Seed}}
[[Image:3ctf.jpg|left|200px]]


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==Crystal structure of oxidized GRX2==
The line below this paragraph, containing "STRUCTURE_3ctf", creates the "Structure Box" on the page.
<StructureSection load='3ctf' size='340' side='right'caption='[[3ctf]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
-->
<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>
{{STRUCTURE_3ctf|  PDB=3ctf  |  SCENE=  }}
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/3ctf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


===Crystal structure of oxidized 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<ref>PMID:20417731</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==About this Structure==
</div>
3CTF is a 1 chain structure of 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].
<div class="pdbe-citations 3ctf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Teng, Y B.]]
[[Category: Teng YB]]
[[Category: Yu, J.]]
[[Category: Yu J]]
[[Category: Zhou, C Z.]]
[[Category: Zhou CZ]]
[[Category: Cytoplasm]]
[[Category: Electron transport]]
[[Category: Mitochondrion]]
[[Category: Oxidized form]]
[[Category: Oxidoreductase]]
[[Category: Redox-active center]]
[[Category: Transit peptide]]
[[Category: Transport]]
 
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Retrieved from "https://proteopedia.org/3ctf"