2ipa
From Proteopedia
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| - | [[Image:2ipa.png|left|200px]] | ||
| - | + | ==solution structure of Trx-ArsC complex== | |
| + | <StructureSection load='2ipa' size='340' side='right'caption='[[2ipa]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ipa]] is a 2 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=2IPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IPA FirstGlance]. <br> | ||
| + | </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=2ipa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ipa OCA], [https://pdbe.org/2ipa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ipa RCSB], [https://www.ebi.ac.uk/pdbsum/2ipa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ipa 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. [[https://www.uniprot.org/uniprot/ARSC_BACSU ARSC_BACSU]] Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances (By similarity). | ||
| + | == 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/ip/2ipa_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=2ipa 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 2ipa" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Thioredoxin|Thioredoxin]] | + | *[[Arsenate reductase 3D structures|Arsenate reductase 3D structures]] |
| - | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | |
| - | == | + | == References == |
| - | < | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Hu, Y | + | </StructureSection> |
| - | [[Category: Jin, C | + | [[Category: Vibrio subtilis ehrenberg 1835]] |
| - | [[Category: Li, Y | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, X | + | [[Category: Hu, Y]] |
| + | [[Category: Jin, C]] | ||
| + | [[Category: Li, Y]] | ||
| + | [[Category: Zhang, X]] | ||
[[Category: Complex]] | [[Category: Complex]] | ||
[[Category: Electron transport-oxidoreductase complex]] | [[Category: Electron transport-oxidoreductase complex]] | ||
[[Category: Solution structure]] | [[Category: Solution structure]] | ||
Current revision
solution structure of Trx-ArsC complex
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