2oe1: Difference between revisions
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==Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (reduced form)== | ==Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (reduced form)== | ||
<StructureSection load='2oe1' size='340' side='right' caption='[[2oe1]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2oe1' size='340' side='right' caption='[[2oe1]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oe0|2oe0]], [[2oe3|2oe3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2oe0|2oe0]], [[2oe3|2oe3]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TRX3 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe1 OCA], [http://pdbe.org/2oe1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oe1 RCSB], [http://www.ebi.ac.uk/pdbsum/2oe1 PDBsum]</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=2oe1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe1 OCA], [http://pdbe.org/2oe1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oe1 RCSB], [http://www.ebi.ac.uk/pdbsum/2oe1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oe1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/2oe1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oe/2oe1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:34, 22 August 2018
Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (reduced form)Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (reduced form)
Structural highlights
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 PubMedThe yeast Saccharomyces cerevisiae Trx3 is a key member of the thioredoxin system to control the cellular redox homeostasis in mitochondria. We solved the crystal structures of yeast Trx3 in oxidized and reduced forms at 1.80 and 2.10 A, respectively. Besides the active site, the additional cysteine residue Cys69 also undergoes a significant redox-correlated conformational change. Comparative structural analyses in combination with activity assays revealed that residue Cys69 could be S-nitrosylated in vitro. S-nitrosylation of Cys69 will decrease the activity of Trx3 by 20%, which is comparable to the effect of the Cys69Ser mutation. Taken together, these findings provided us some new insights into the putative function of the additional cysteine residues of Trx3. Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues.,Bao R, Zhang Y, Zhou CZ, Chen Y Biochim Biophys Acta. 2009 Apr;1794(4):716-21. Epub 2009 Jan 3. PMID:19166985[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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