6xiv: Difference between revisions
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==SeMet-Rns, in complex with potential inhibitor== | ==SeMet-Rns, in complex with potential inhibitor== | ||
<StructureSection load='6xiv' size='340' side='right'caption='[[6xiv]]' scene=''> | <StructureSection load='6xiv' size='340' side='right'caption='[[6xiv]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XIV FirstGlance]. <br> | <table><tr><td colspan='2'>[[6xiv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XIV 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=6xiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xiv OCA], [https://pdbe.org/6xiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xiv RCSB], [https://www.ebi.ac.uk/pdbsum/6xiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xiv ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rns ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=6xiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xiv OCA], [https://pdbe.org/6xiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xiv RCSB], [https://www.ebi.ac.uk/pdbsum/6xiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xiv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/RNS_ECOLX RNS_ECOLX]] Required for the expression of the CS1 and CS2 adhesins of enterotoxygenic E.coli. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Enteric infections caused by the gram-negative bacteria enterotoxigenic Escherichia coli (ETEC), Vibrio cholerae, Shigella flexneri, and Salmonella enterica are among the most common and affect billions of people each year. These bacteria control expression of virulence factors using a network of transcriptional regulators, some of which are modulated by small molecules as has been shown for ToxT, an AraC family member from V. cholerae. In ETEC the expression of many types of adhesive pili is dependent upon the AraC family member Rns. We present here the 3 A crystal structure of Rns and show it closely resembles ToxT. Rns crystallized as a dimer via an interface similar to that observed in other dimeric AraC's. Furthermore, the structure of Rns revealed the presence of a ligand, decanoic acid, that inhibits its activity in a manner similar to the fatty acid mediated inhibition observed for ToxT and the S. enterica homologue HilD. Together, these results support our hypothesis that fatty acids regulate virulence controlling AraC family members in a common manner across a number of enteric pathogens. Furthermore, for the first time this work identifies a small molecule capable of inhibiting the ETEC Rns regulon, providing a basis for development of therapeutics against this deadly human pathogen. | |||
Structure of the master regulator Rns reveals an inhibitor of enterotoxigenic Escherichia coli virulence regulons.,Midgett CR, Talbot KM, Day JL, Munson GP, Kull FJ Sci Rep. 2021 Aug 2;11(1):15663. doi: 10.1038/s41598-021-95123-2. PMID:34341412<ref>PMID:34341412</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6xiv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kull | [[Category: Kull, F J]] | ||
[[Category: Midgett | [[Category: Midgett, C R]] | ||
[[Category: Dna binding protein]] | |||
[[Category: Dna binding protein-inhibitor complex]] | |||
[[Category: Etec]] | |||
[[Category: Inhibitor]] | |||
[[Category: Rn]] | |||
[[Category: Transcription factor]] | |||
Latest revision as of 10:07, 2 February 2022
SeMet-Rns, in complex with potential inhibitorSeMet-Rns, in complex with potential inhibitor
Structural highlights
Function[RNS_ECOLX] Required for the expression of the CS1 and CS2 adhesins of enterotoxygenic E.coli. Publication Abstract from PubMedEnteric infections caused by the gram-negative bacteria enterotoxigenic Escherichia coli (ETEC), Vibrio cholerae, Shigella flexneri, and Salmonella enterica are among the most common and affect billions of people each year. These bacteria control expression of virulence factors using a network of transcriptional regulators, some of which are modulated by small molecules as has been shown for ToxT, an AraC family member from V. cholerae. In ETEC the expression of many types of adhesive pili is dependent upon the AraC family member Rns. We present here the 3 A crystal structure of Rns and show it closely resembles ToxT. Rns crystallized as a dimer via an interface similar to that observed in other dimeric AraC's. Furthermore, the structure of Rns revealed the presence of a ligand, decanoic acid, that inhibits its activity in a manner similar to the fatty acid mediated inhibition observed for ToxT and the S. enterica homologue HilD. Together, these results support our hypothesis that fatty acids regulate virulence controlling AraC family members in a common manner across a number of enteric pathogens. Furthermore, for the first time this work identifies a small molecule capable of inhibiting the ETEC Rns regulon, providing a basis for development of therapeutics against this deadly human pathogen. Structure of the master regulator Rns reveals an inhibitor of enterotoxigenic Escherichia coli virulence regulons.,Midgett CR, Talbot KM, Day JL, Munson GP, Kull FJ Sci Rep. 2021 Aug 2;11(1):15663. doi: 10.1038/s41598-021-95123-2. PMID:34341412[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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