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| | ==Crystal Structure of Salmonella enterica serovar Typhimurium DsbA== | | ==Crystal Structure of Salmonella enterica serovar Typhimurium DsbA== |
| - | <StructureSection load='3l9s' size='340' side='right' caption='[[3l9s]], [[Resolution|resolution]] 1.58Å' scene=''> | + | <StructureSection load='3l9s' size='340' side='right'caption='[[3l9s]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3l9s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Salts Salts]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l9s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._SL1344 Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L9S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3h93|3h93]], [[3a3t|3a3t]], [[3f4r|3f4r]], [[3bci|3bci]], [[1fvk|1fvk]], [[1dsb|1dsb]], [[3l9u|3l9u]], [[3l9v|3l9v]]</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]] 1.58Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbA, STM3997 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216597 SALTS])</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=3l9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l9s OCA], [https://pdbe.org/3l9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l9s RCSB], [https://www.ebi.ac.uk/pdbsum/3l9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l9s ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=3l9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l9s OCA], [http://pdbe.org/3l9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l9s RCSB], [http://www.ebi.ac.uk/pdbsum/3l9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l9s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DSBA_SALTY DSBA_SALTY] Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l9/3l9s_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l9/3l9s_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Protein disulfide-isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Salts]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]] |
| - | [[Category: Guncar, G]] | + | [[Category: Guncar G]] |
| - | [[Category: Heras, B]] | + | [[Category: Heras B]] |
| - | [[Category: Jarrott, R]] | + | [[Category: Jarrott R]] |
| - | [[Category: Shouldice, S R]] | + | [[Category: Shouldice SR]] |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Dsba]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Thiol-disulfide oxidoreductase]]
| + | |
| - | [[Category: Thioredoxin-fold]]
| + | |
| Structural highlights
Function
DSBA_SALTY Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity).
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
In prototypic Escherichia coli K-12 the introduction of disulfide bonds into folding proteins is mediated by the Dsb family of enzymes, primarily through the actions of the highly oxidizing protein EcDsbA. Homologues of the Dsb catalysts are found in most bacteria. Interestingly, pathogens have developed distinct Dsb machineries that play a pivotal role in the biogenesis of virulence factors, hence contributing to their pathogenicity. Salmonella enterica serovar (sv.) Typhimurium encodes an extended number of sulfhydryl oxidases, namely SeDsbA, SeDsbL, and SeSrgA. Here we report a comprehensive analysis of the sv. Typhimurium thiol oxidative system through the structural and functional characterization of the three Salmonella DsbA paralogues. The three proteins share low sequence identity, which results in several unique three-dimensional characteristics, principally in areas involved in substrate binding and disulfide catalysis. Furthermore, the Salmonella DsbA-like proteins also have different redox properties. Whereas functional characterization revealed some degree of redundancy, the properties of SeDsbA, SeDsbL, and SeSrgA and their expression pattern in sv. Typhimurium indicate a diverse role for these enzymes in virulence.
Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium.,Heras B, Totsika M, Jarrott R, Shouldice SR, Guncar G, Achard ME, Wells TJ, Argente MP, McEwan AG, Schembri MA J Biol Chem. 2010 Jun 11;285(24):18423-32. Epub 2010 Mar 16. PMID:20233716[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heras B, Totsika M, Jarrott R, Shouldice SR, Guncar G, Achard ME, Wells TJ, Argente MP, McEwan AG, Schembri MA. Structural and functional characterization of three DsbA paralogues from Salmonella enterica serovar typhimurium. J Biol Chem. 2010 Jun 11;285(24):18423-32. Epub 2010 Mar 16. PMID:20233716 doi:10.1074/jbc.M110.101360
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