5lrs: Difference between revisions

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New page: '''Unreleased structure''' The entry 5lrs is ON HOLD Authors: Hall, M., Grundstrom, C., Begum, A., Lindberg, M., Sauer, U.H., Almqvist, F., Johansson, J., Sauer-Eriksson, A.E. Descript...
 
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'''Unreleased structure'''


The entry 5lrs is ON HOLD
==The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30-bp operator PrfA-box motif==
<StructureSection load='5lrs' size='340' side='right'caption='[[5lrs]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lrs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LRS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></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=5lrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lrs OCA], [https://pdbe.org/5lrs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lrs RCSB], [https://www.ebi.ac.uk/pdbsum/5lrs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lrs ProSAT]</span></td></tr>
</table>
== 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;">
== Publication Abstract from PubMed ==
Infection 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.


Authors: Hall, M., Grundstrom, C., Begum, A., Lindberg, M., Sauer, U.H., Almqvist, F., Johansson, J., Sauer-Eriksson, A.E.
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<ref>PMID:27930316</ref>


Description: The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30-bp operator PrfA-box motif
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Johansson, J]]
<div class="pdbe-citations 5lrs" style="background-color:#fffaf0;"></div>
[[Category: Sauer-Eriksson, A.E]]
 
[[Category: Grundstrom, C]]
==See Also==
[[Category: Lindberg, M]]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
[[Category: Almqvist, F]]
== References ==
[[Category: Hall, M]]
<references/>
[[Category: Begum, A]]
__TOC__
[[Category: Sauer, U.H]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria monocytogenes]]
[[Category: Almqvist F]]
[[Category: Begum A]]
[[Category: Grundstrom C]]
[[Category: Hall M]]
[[Category: Johansson J]]
[[Category: Lindberg M]]
[[Category: Sauer UH]]
[[Category: Sauer-Eriksson AE]]

Latest revision as of 21:43, 18 October 2023

The Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30-bp operator PrfA-box motifThe Transcriptional Regulator PrfA from Listeria Monocytogenes in complex with glutathione and a 30-bp operator PrfA-box motif

Structural highlights

5lrs is a 4 chain structure with sequence from Listeria monocytogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRFA_LISMO Positively regulates expression of listeriolysin, of 1-phosphadidylinositol phosphodiesterase (PI-PLC) and other virulence factors.

Publication Abstract from PubMed

Infection 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 Also

References

  1. Hall M, Grundstrom C, Begum A, Lindberg MJ, Sauer UH, Almqvist F, Johansson J, Sauer-Eriksson AE. Structural basis for glutathione-mediated activation of the virulence regulatory protein PrfA in Listeria. 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 doi:http://dx.doi.org/10.1073/pnas.1614028114

5lrs, resolution 2.90Å

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