3szt

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Current revision (09:58, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3szt' size='340' side='right'caption='[[3szt]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
<StructureSection load='3szt' size='340' side='right'caption='[[3szt]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3szt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3szt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OHN:N-3-OXO-DODECANOYL-L-HOMOSERINE+LACTONE'>OHN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA1898, qscR ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OHN:N-3-OXO-DODECANOYL-L-HOMOSERINE+LACTONE'>OHN</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=3szt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szt OCA], [https://pdbe.org/3szt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szt RCSB], [https://www.ebi.ac.uk/pdbsum/3szt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szt ProSAT]</span></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=3szt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3szt OCA], [https://pdbe.org/3szt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3szt RCSB], [https://www.ebi.ac.uk/pdbsum/3szt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3szt ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9RMS5_PSEAI Q9RMS5_PSEAI]
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Acyl-homoserine lactone (AHL) quorum sensing controls gene expression in hundreds of Proteobacteria including a number of plant and animal pathogens. Generally, the AHL receptors are members of a family of related transcription factors, and although they have been targets for development of antivirulence therapeutics there is very little structural information about this class of bacterial receptors. We have determined the structure of the transcription factor, QscR, bound to N-3-oxo-dodecanoyl-homoserine lactone from the opportunistic human pathogen Pseudomonas aeruginosa at a resolution of 2.55 A. The ligand-bound QscR is a dimer with a unique symmetric "cross-subunit" arrangement containing multiple dimerization interfaces involving both domains of each subunit. The QscR dimer appears poised to bind DNA. Predictions about signal binding and dimerization contacts were supported by studies of mutant QscR proteins in vivo. The acyl chain of the AHL is in close proximity to the dimerization interfaces. Our data are consistent with an allosteric mechanism of signal transmission in the regulation of DNA binding and thus virulence gene expression.
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Crystal structure of QscR, a Pseudomonas aeruginosa quorum sensing signal receptor.,Lintz MJ, Oinuma K, Wysoczynski CL, Greenberg EP, Churchill ME Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15763-8. Epub 2011 Sep 12. PMID:21911405<ref>PMID:21911405</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3szt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Churchill, M E.A]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Lintz, M J]]
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[[Category: Churchill MEA]]
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[[Category: 3-oxo-c12 hsl]]
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[[Category: Lintz MJ]]
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[[Category: Helix-turn-helix]]
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[[Category: Quorum sensing acyl-homoserine lactone]]
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[[Category: Transcription]]
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[[Category: Transcription factor]]
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Current revision

Quorum Sensing Control Repressor, QscR, Bound to N-3-oxo-dodecanoyl-L-Homoserine Lactone

PDB ID 3szt

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