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==Solution structure of desulfothioredoxin from Desulfovibrio vulgaris Hildenborough in its reduced form==
==Solution structure of desulfothioredoxin from Desulfovibrio vulgaris Hildenborough in its reduced form==
<StructureSection load='2l6d' size='340' side='right'caption='[[2l6d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2l6d' size='340' side='right'caption='[[2l6d]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2l6d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desvh Desvh]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6D FirstGlance]. <br>
<table><tr><td colspan='2'>[[2l6d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfovibrio_vulgaris_str._Hildenborough Desulfovibrio vulgaris str. Hildenborough]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L6D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l6c|2l6c]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DVU_0378 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=882 DESVH])</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=2l6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6d OCA], [https://pdbe.org/2l6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6d RCSB], [https://www.ebi.ac.uk/pdbsum/2l6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6d 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=2l6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l6d OCA], [https://pdbe.org/2l6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l6d RCSB], [https://www.ebi.ac.uk/pdbsum/2l6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l6d ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q72F37_DESVH Q72F37_DESVH]
Cytoplasmic desulfothioredoxin (Dtrx) from the anaerobe Desulfovibrio vulgaris Hildenborough has been identified as a new member of the thiol disulfide oxidoreductase family. The active site of Dtrx contains a particular consensus sequence, CPHC, never seen in the cytoplasmic thioredoxins and generally found in periplasmic oxidases. Unlike canonical thioredoxins (Trx), Dtrx does not present any disulfide reductase activity but it presents instead an unusual disulfide isomerase activity. We have used NMR spectroscopy to gain insights into the structure and the catalytic mechanism of this unusual Dtrx. The redox potential of Dtrx (-181 mV) is significantly less reducing than that of canonical Trx. A pH dependence study allowed the determination of the pKa of all protonable residues, including the cysteine and histidine residues. Thus, the pKa for the thiol group of C31 and C34 is 4.8 and 11.3, respectively. The H33 pKa value, experimentally determined for the first time, differs notably as a function of the redox states, 7.2 for the reduced state and 4.6 for the oxidized state. These data suggest an important role of H33 in the molecular mechanism of Dtrx catalysis which is confirmed by the properties of mutant DtrxH33G protein. The NMR structure of Dtrx shows a different charge repartition compared to canonical Trx. The results presented are likely indicative of the involvement of this protein in the catalysis of substrates specific of the anaerobe cytoplasm of DvH. The study of Dtrx is an important step toward revealing the molecular details of the thiol-disulfide oxidoreductase catalytic mechanism.
 
Structural and mechanistic insights into an unusual thiol disulfide oxidoreductase.,Garcin EB, Bornet O, Elantak L, Vita N, Pieulle L, Guerlesquin F, Sebban-Kreuzer C J Biol Chem. 2011 Nov 28. PMID:22128175<ref>PMID:22128175</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2l6d" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Desvh]]
[[Category: Desulfovibrio vulgaris str. Hildenborough]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bornet, O]]
[[Category: Bornet O]]
[[Category: Garcin, E B]]
[[Category: Garcin EB]]
[[Category: Guerlesquin, F]]
[[Category: Guerlesquin F]]
[[Category: Sebban-Kreuzer, C]]
[[Category: Sebban-Kreuzer C]]
[[Category: Oxidoreductase]]
[[Category: Thioredoxin fold]]

Latest revision as of 06:53, 1 May 2024

Solution structure of desulfothioredoxin from Desulfovibrio vulgaris Hildenborough in its reduced form

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