|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Crystal structure of oxidized GRX2== | | ==Crystal structure of oxidized GRX2== |
| - | <StructureSection load='3ctf' size='340' side='right' caption='[[3ctf]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3ctf' size='340' side='right'caption='[[3ctf]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ctf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CTF FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ctg|3ctg]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRX2, TTR, TTR1, YDR513W, D9719.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arsenate_reductase_(glutaredoxin) Arsenate reductase (glutaredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.20.4.1 1.20.4.1] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ctf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctf OCA], [http://pdbe.org/3ctf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ctf RCSB], [http://www.ebi.ac.uk/pdbsum/3ctf PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ct/3ctf_consurf.spt"</scriptWhenChecked> | + | <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/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
| Line 33: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Teng, Y B]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Yu, J]] | + | [[Category: Teng YB]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Yu J]] |
| - | [[Category: Electron transport]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Mitochondrion]]
| + | |
| - | [[Category: Oxidized form]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Transit peptide]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
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.[1] [2] [3]
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Luikenhuis S, Perrone G, Dawes IW, Grant CM. The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species. Mol Biol Cell. 1998 May;9(5):1081-91. PMID:9571241
- ↑ Collinson EJ, Wheeler GL, Garrido EO, Avery AM, Avery SV, Grant CM. The yeast glutaredoxins are active as glutathione peroxidases. J Biol Chem. 2002 May 10;277(19):16712-7. Epub 2002 Mar 1. PMID:11875065 doi:http://dx.doi.org/10.1074/jbc.M111686200
- ↑ Collinson EJ, Grant CM. Role of yeast glutaredoxins as glutathione S-transferases. J Biol Chem. 2003 Jun 20;278(25):22492-7. Epub 2003 Apr 8. PMID:12684511 doi:http://dx.doi.org/10.1074/jbc.M301387200
- ↑ Li WF, Yu J, Ma XX, Teng YB, Luo M, Tang YJ, Zhou CZ. Structural basis for the different activities of yeast Grx1 and Grx2. Biochim Biophys Acta. 2010 Jul;1804(7):1542-7. Epub 2010 Apr 24. PMID:20417731 doi:10.1016/j.bbapap.2010.04.010
|
