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6hck
From Proteopedia
(Difference between revisions)
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<StructureSection load='6hck' size='340' side='right' caption='[[6hck]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='6hck' size='340' side='right' caption='[[6hck]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6hck]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HCK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hck]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HCK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HCK FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prfA, lmo0200 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</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=6hck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hck OCA], [http://pdbe.org/6hck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hck RCSB], [http://www.ebi.ac.uk/pdbsum/6hck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hck ProSAT]</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=6hck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hck OCA], [http://pdbe.org/6hck PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hck RCSB], [http://www.ebi.ac.uk/pdbsum/6hck PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hck ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/PRFA_LISMO PRFA_LISMO]] Positively regulates expression of listeriolysin, of 1-phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors. | [[http://www.uniprot.org/uniprot/PRFA_LISMO PRFA_LISMO]] Positively regulates expression of listeriolysin, of 1-phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | To optimize fitness, pathogens selectively activate their virulence program upon host entry. Here, we report that the facultative intracellular bacterium Listeria monocytogenes exploits exogenous oligopeptides, a ubiquitous organic N source, to sense the environment and control the activity of its virulence transcriptional activator, PrfA. Using a genetic screen in adsorbent-treated (PrfA-inducing) medium, we found that PrfA is functionally regulated by the balance between activating and inhibitory nutritional peptides scavenged via the Opp transport system. Activating peptides provide essential cysteine precursor for the PrfA-inducing cofactor glutathione (GSH). Non-cysteine-containing peptides cause promiscuous PrfA inhibition. Biophysical and co-crystallization studies reveal that peptides inhibit PrfA through steric blockade of the GSH binding site, a regulation mechanism directly linking bacterial virulence and metabolism. L. monocytogenes mutant analysis in macrophages and our functional data support a model in which changes in the balance of antagonistic Opp-imported oligopeptides promote PrfA induction intracellularly and PrfA repression outside the host. | ||
| + | |||
| + | Control of Bacterial Virulence through the Peptide Signature of the Habitat.,Krypotou E, Scortti M, Grundstrom C, Oelker M, Luisi BF, Sauer-Eriksson AE, Vazquez-Boland J Cell Rep. 2019 Feb 12;26(7):1815-1827.e5. doi: 10.1016/j.celrep.2019.01.073. PMID:30759392<ref>PMID:30759392</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6hck" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Lismo]] | ||
[[Category: Grundstrom, C]] | [[Category: Grundstrom, C]] | ||
[[Category: Krypotou, E]] | [[Category: Krypotou, E]] | ||
Revision as of 16:00, 27 February 2019
The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with dipeptide Leu-Leu
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