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| | <StructureSection load='2h1b' size='340' side='right'caption='[[2h1b]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='2h1b' size='340' side='right'caption='[[2h1b]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2h1b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2h1b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1su9|1su9]], [[1st9|1st9]], [[2h19|2h19]], [[2h1a|2h1a]], [[2h1d|2h1d]], [[2h1g|2h1g]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">resA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=2h1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1b OCA], [https://pdbe.org/2h1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1b RCSB], [https://www.ebi.ac.uk/pdbsum/2h1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1b 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=2h1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1b OCA], [https://pdbe.org/2h1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1b RCSB], [https://www.ebi.ac.uk/pdbsum/2h1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RESA_BACSU RESA_BACSU]] Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.<ref>PMID:12637552</ref>
| + | [https://www.uniprot.org/uniprot/RESA_BACSU RESA_BACSU] Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.<ref>PMID:12637552</ref> |
| | == 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: Brun, N E.Le]] | + | [[Category: Crow A]] |
| - | [[Category: Crow, A]] | + | [[Category: Le Brun NE]] |
| - | [[Category: Lewin, A]] | + | [[Category: Lewin A]] |
| - | [[Category: Oubrie, A]] | + | [[Category: Oubrie A]] |
| - | [[Category: E80q]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Resa]]
| + | |
| - | [[Category: Resa e80q]]
| + | |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
RESA_BACSU Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.[1]
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
ResA, an extracytoplasmic thioredoxin from Bacillus subtilis, acts in cytochrome c maturation by reducing the disulfide bond present in apocytochromes prior to covalent attachment of heme. This reaction is (and has to be) specific, as broad substrate specificity would result in unproductive shortcircuiting with the general oxidizing thioredoxin(s) present in the same compartment. Using mutational analysis and subsequent biochemical and structural characterization of active site variants, we show that reduced ResA displays unusually low reactivity at neutral pH, consistent with the observed high pKa values>8 for both active site cysteines. Residue Glu80 is shown to play a key role in controlling the acid-base properties of the active site. A model in which substrate binding dramatically enhances the reactivity of the active site cysteines is proposed to account for the specificity of the protein. Such a substratemediated activation mechanism is likely to have wide relevance for extracytoplasmic thioredoxins.
Molecular basis for specificity of the extracytoplasmic thioredoxin ResA.,Lewin A, Crow A, Oubrie A, Le Brun NE J Biol Chem. 2006 Nov 17;281(46):35467-77. Epub 2006 Sep 13. PMID:16971393[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Erlendsson LS, Acheson RM, Hederstedt L, Le Brun NE. Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. J Biol Chem. 2003 May 16;278(20):17852-8. Epub 2003 Mar 7. PMID:12637552 doi:http://dx.doi.org/10.1074/jbc.M300103200
- ↑ Lewin A, Crow A, Oubrie A, Le Brun NE. Molecular basis for specificity of the extracytoplasmic thioredoxin ResA. J Biol Chem. 2006 Nov 17;281(46):35467-77. Epub 2006 Sep 13. PMID:16971393 doi:10.1074/jbc.M607047200
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