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| | ==solution structures of the reduced form of thioredoxin from Bacillus subtilis== | | ==solution structures of the reduced form of thioredoxin from Bacillus subtilis== |
| - | <StructureSection load='2gzy' size='340' side='right'caption='[[2gzy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2gzy' size='340' side='right'caption='[[2gzy]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gzy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GZY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gzy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gzz|2gzz]]</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='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=2gzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzy OCA], [http://pdbe.org/2gzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gzy RCSB], [http://www.ebi.ac.uk/pdbsum/2gzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzy 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=2gzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzy OCA], [https://pdbe.org/2gzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gzy RCSB], [https://www.ebi.ac.uk/pdbsum/2gzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzy ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/THIO_BACSU THIO_BACSU]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | + | [https://www.uniprot.org/uniprot/THIO_BACSU THIO_BACSU] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, J]] | + | [[Category: Chen J]] |
| - | [[Category: Jin, C]] | + | [[Category: Jin C]] |
| - | [[Category: Xu, H]] | + | [[Category: Xu H]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang X]] |
| - | [[Category: Alpha/beta]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| Structural highlights
Function
THIO_BACSU Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
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
Arsenic compounds commonly exist in nature and are toxic to nearly all kinds of life forms, which directed the evolution of enzymes in many organisms for arsenic detoxification. In bacteria, the thioredoxin-coupled arsenate reductase catalyzes the reduction of arsenate to arsenite by intramolecular thiol-disulfide cascade. The oxidized arsenate reductase ArsC is subsequently regenerated by thioredoxin through an intermolecular thiol-disulfide exchange process. The solution structure of the Bacillus subtilis thioredoxin-arsenate reductase complex represents the transiently formed intermediate during the intermolecular thiol-disulfide exchange reaction. A comparison of the complex structure with that of thioredoxin and arsenate reductase proteins in redox states showed substantial conformational changes coupled to the reaction process, with arsenate reductase, especially, adopting an "intermediate" conformation in the complex. Our current studies provide novel insights into understanding the reaction mechanisms of the thioredoxin-arsenate reductase pathway.
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.,Li Y, Hu Y, Zhang X, Xu H, Lescop E, Xia B, Jin C J Biol Chem. 2007 Apr 13;282(15):11078-83. Epub 2007 Feb 15. PMID:17303556[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, Hu Y, Zhang X, Xu H, Lescop E, Xia B, Jin C. Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis. J Biol Chem. 2007 Apr 13;282(15):11078-83. Epub 2007 Feb 15. PMID:17303556 doi:http://dx.doi.org/10.1074/jbc.M700970200
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