5lek: Difference between revisions
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<StructureSection load='5lek' size='340' side='right'caption='[[5lek]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='5lek' size='340' side='right'caption='[[5lek]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lek]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LEK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5lek]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] and [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LEK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lek OCA], [https://pdbe.org/5lek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lek RCSB], [https://www.ebi.ac.uk/pdbsum/5lek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lek ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[ | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Almqvist | [[Category: Listeria monocytogenes]] | ||
[[Category: Begum | [[Category: Listeria monocytogenes EGD-e]] | ||
[[Category: Grundstrom | [[Category: Almqvist F]] | ||
[[Category: Hall | [[Category: Begum A]] | ||
[[Category: Johansson | [[Category: Grundstrom C]] | ||
[[Category: Lindberg | [[Category: Hall M]] | ||
[[Category: Sauer | [[Category: Johansson J]] | ||
[[Category: Sauer-Eriksson | [[Category: Lindberg M]] | ||
[[Category: Sauer UH]] | |||
[[Category: Sauer-Eriksson AE]] | |||
Latest revision as of 11:57, 11 October 2023
The Transcriptional Regulator PrfA-G145S mutant from Listeria Monocytogenes in complex with a 30-bp operator PrfA-box motifThe Transcriptional Regulator PrfA-G145S mutant from Listeria Monocytogenes in complex with a 30-bp operator PrfA-box motif
Structural highlights
FunctionPRFA_LISMO Positively regulates expression of listeriolysin, of 1-phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors. Publication Abstract from PubMedInfection by the human bacterial pathogen Listeria monocytogenes is mainly controlled by the positive regulatory factor A (PrfA), a member of the Crp/Fnr family of transcriptional activators. Published data suggest that PrfA requires the binding of a cofactor for full activity, and it was recently proposed that glutathione (GSH) could fulfill this function. Here we report the crystal structures of PrfA in complex with GSH and in complex with GSH and its cognate DNA, the hly operator PrfA box motif. These structures reveal the structural basis for a GSH-mediated allosteric mode of activation of PrfA in the cytosol of the host cell. The crystal structure of PrfAWT in complex only with DNA confirms that PrfAWT can adopt a DNA binding-compatible structure without binding the GSH activator molecule. By binding to PrfA in the cytosol of the host cell, GSH induces the correct fold of the HTH motifs, thus priming the PrfA protein for DNA interaction. Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria.,Hall M, Grundstrom C, Begum A, Lindberg MJ, Sauer UH, Almqvist F, Johansson J, Sauer-Eriksson AE Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14733-14738. doi:, 10.1073/pnas.1614028114. Epub 2016 Dec 5. PMID:27930316[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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