|
|
Line 1: |
Line 1: |
| | | |
| ==Crystal Structure of Salmonella enterica serovar Typhimurium SrgA== | | ==Crystal Structure of Salmonella enterica serovar Typhimurium SrgA== |
- | <StructureSection load='3l9v' size='340' side='right' caption='[[3l9v]], [[Resolution|resolution]] 2.15Å' scene=''> | + | <StructureSection load='3l9v' size='340' side='right'caption='[[3l9v]], [[Resolution|resolution]] 2.15Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3l9v]] is a 5 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=3L9V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L9V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l9v]] is a 5 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=3L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L9V FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</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]] 2.151Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene></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]], [[3l9s|3l9s]], [[3l9u|3l9u]]</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=3l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l9v OCA], [https://pdbe.org/3l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l9v RCSB], [https://www.ebi.ac.uk/pdbsum/3l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l9v ProSAT]</span></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSLT011, srgA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216597 SALTS])</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=3l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l9v OCA], [http://pdbe.org/3l9v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3l9v RCSB], [http://www.ebi.ac.uk/pdbsum/3l9v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3l9v ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q04815_SALTM Q04815_SALTM] |
| == 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/l9/3l9v_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l9/3l9v_consurf.spt"</scriptWhenChecked> |
- | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
Line 34: |
Line 33: |
| __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: Isomerase]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Srga]]
| + | |
- | [[Category: Thiol-disulfide oxidoreductase]]
| + | |
- | [[Category: Thioredoxin-fold]]
| + | |
| Structural highlights
Function
Q04815_SALTM
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
|