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2gzz
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2gzz" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gzz" /> '''solution structures of the oxidized form of ...) |
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| - | [[Image:2gzz.jpg|left|200px]]<br /><applet load="2gzz" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2gzz" /> | ||
| - | '''solution structures of the oxidized form of thioredoxin from Bacillus subtilis'''<br /> | ||
| - | == | + | ==solution structures of the oxidized form of thioredoxin from Bacillus subtilis== |
| - | + | <StructureSection load='2gzz' size='340' side='right'caption='[[2gzz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2gzz]] is a 1 chain structure with sequence from [https://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=2GZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZZ 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;'>[[2gzy|2gzy]]</div></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=2gzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gzz OCA], [https://pdbe.org/2gzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gzz RCSB], [https://www.ebi.ac.uk/pdbsum/2gzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gzz ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| - | [ | + | [[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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/2gzz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=2gzz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:17303556</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2gzz" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Vibrio subtilis ehrenberg 1835]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen, J]] | ||
| + | [[Category: Jin, C]] | ||
| + | [[Category: Xu, H]] | ||
| + | [[Category: Zhang, X]] | ||
| + | [[Category: Alpha/beta]] | ||
| + | [[Category: Electron transport]] | ||
Current revision
solution structures of the oxidized form of thioredoxin from Bacillus subtilis
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