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| | <StructureSection load='3itj' size='340' side='right'caption='[[3itj]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3itj' size='340' side='right'caption='[[3itj]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3itj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_w303 Saccharomyces cerevisiae w303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ITJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3itj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_W303 Saccharomyces cerevisiae W303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ITJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ITJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">D9476.5, TRR1, YDR353W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580240 Saccharomyces cerevisiae W303])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] </span></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=3itj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3itj OCA], [https://pdbe.org/3itj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3itj RCSB], [https://www.ebi.ac.uk/pdbsum/3itj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3itj ProSAT]</span></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=3itj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3itj OCA], [https://pdbe.org/3itj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3itj RCSB], [https://www.ebi.ac.uk/pdbsum/3itj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3itj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TRXB1_YEAST TRXB1_YEAST]] Acts on thioredoxins 1 and 2.
| + | [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]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Saccharomyces cerevisiae w303]] | + | [[Category: Saccharomyces cerevisiae W303]] |
| - | [[Category: Thioredoxin-disulfide reductase]]
| + | [[Category: Alves SV]] |
| - | [[Category: Alves, S V]] | + | [[Category: Discola KF]] |
| - | [[Category: Discola, K F]] | + | [[Category: Guimaraes BG]] |
| - | [[Category: Guimaraes, B G]] | + | [[Category: Medrano FJ]] |
| - | [[Category: Medrano, F J]] | + | [[Category: Netto LES]] |
| - | [[Category: Netto, L E.S]] | + | [[Category: Oliveira MA]] |
| - | [[Category: Oliveira, M A]] | + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Thioredoxin reductase 1 alpha/beta type protein]]
| + | |
| Structural highlights
Function
TRXB1_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 PubMed
The enzymatic activity of thioredoxin reductase enzymes is endowed by at least two redox centers: a flavin and a dithiol/disulfide CXXC motif. The interaction between thioredoxin reductase and thioredoxin is generally species-specific, but the molecular aspects related to this phenomenon remain elusive. Here, we investigated the yeast cytosolic thioredoxin system, which is composed of NADPH, thioredoxin reductase (ScTrxR1), and thioredoxin 1 (ScTrx1) or thioredoxin 2 (ScTrx2). We showed that ScTrxR1 was able to efficiently reduce yeast thioredoxins (mitochondrial and cytosolic) but failed to reduce the human and Escherichia coli thioredoxin counterparts. To gain insights into this specificity, the crystallographic structure of oxidized ScTrxR1 was solved at 2.4 A resolution. The protein topology of the redox centers indicated the necessity of a large structural rearrangement for FAD and thioredoxin reduction using NADPH. Therefore, we modeled a large structural rotation between the two ScTrxR1 domains (based on the previously described crystal structure, PDB code 1F6M ). Employing diverse approaches including enzymatic assays, site-directed mutagenesis, amino acid sequence alignment, and structure comparisons, insights were obtained about the features involved in the species-specificity phenomenon, such as complementary electronic parameters between the surfaces of ScTrxR1 and yeast thioredoxin enzymes and loops and residues (such as Ser(72) in ScTrx2). Finally, structural comparisons and amino acid alignments led us to propose a new classification that includes a larger number of enzymes with thioredoxin reductase activity, neglected in the low/high molecular weight classification.
Insights into the Specificity of Thioredoxin Reductase-Thioredoxin Interactions. A Structural and Functional Investigation of the Yeast Thioredoxin System.,Oliveira MA, Discola KF, Alves SV, Medrano FJ, Guimaraes BG, Netto LE Biochemistry. 2010 Mar 26. PMID:20235561[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oliveira MA, Discola KF, Alves SV, Medrano FJ, Guimaraes BG, Netto LE. Insights into the Specificity of Thioredoxin Reductase-Thioredoxin Interactions. A Structural and Functional Investigation of the Yeast Thioredoxin System. Biochemistry. 2010 Mar 26. PMID:20235561 doi:10.1021/bi901962p
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