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==Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1== | ==Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1== | ||
<StructureSection load='3d8x' size='340' side='right' caption='[[3d8x]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3d8x' size='340' side='right'caption='[[3d8x]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3d8x]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3d8x]] is a 2 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=3D8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D8X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></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=3d8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d8x OCA], [https://pdbe.org/3d8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d8x RCSB], [https://www.ebi.ac.uk/pdbsum/3d8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d8x ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TRXB1_YEAST TRXB1_YEAST] Acts on thioredoxins 1 and 2. | ||
== 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/d8/3d8x_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d8/3d8x_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <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> | ||
</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/ | </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=3d8x ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 28: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3d8x" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Thioredoxin | *[[Thioredoxin reductase 3D structures|Thioredoxin reductase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Bao | [[Category: Bao R]] | ||
[[Category: Chen | [[Category: Chen YX]] | ||
[[Category: Yu | [[Category: Yu J]] | ||
[[Category: Zhang | [[Category: Zhang ZY]] | ||
[[Category: Zhou | [[Category: Zhou C-Z]] | ||
Latest revision as of 08:45, 17 October 2024
Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1
Structural highlights
FunctionTRXB1_YEAST Acts on thioredoxins 1 and 2. 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 PubMedThioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide oxidoreductase family of the flavoenzymes. It can use a dithiol-disulfide active-site to transfer reducing equivalents from NADPH to thioredoxin (Trx), via the cofactor FAD. In Saccharomyces cerevisiae, the cytoplasmic thioredoxin reductase Trr1 plays an important role in multiple cellular events under the control of transcription factor Yap1 and/or Rho5. Here we present the crystal structure of Trr1 at the resolution of 2.8 A, the first fungal TrxR structure. Structural analysis shows it shares a very similar overall structure to Escherichia coli TrxR. However, fine comparisons indicate some distinct differences at the Trx recognition sites. These differences might be responsible to the species-specific recognition of Trx, which has been demonstrated by previous biochemical assays. Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin.,Zhang Z, Bao R, Zhang Y, Yu J, Zhou CZ, Chen Y Biochim Biophys Acta. 2009 Jan;1794(1):124-8. Epub 2008 Oct 1. PMID:18930846[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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