View source for 6pcp


==Mechanism for regulation of DNA binding of Bordetella bronchiseptica BpsR by 6-hydroxynicotinic acid==
<StructureSection load='6pcp' size='340' side='right'caption='[[6pcp]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pcp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PCP 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OA7:6-hydroxypyridine-3-carboxylic+acid'>OA7</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=6pcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pcp OCA], [https://pdbe.org/6pcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pcp RCSB], [https://www.ebi.ac.uk/pdbsum/6pcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pcp ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Bordetella bacteria are respiratory pathogens of humans, birds, and livestock. Bordetella pertussis the causative agent of whopping cough remains a significant health issue. The transcriptional regulator, BpsR, represses a number of Bordetella genes relating to virulence, cell adhesion, cell motility, and nicotinic acid metabolism. DNA binding of BpsR is allosterically regulated by interaction with 6-hydroxynicotinic acid (6HNA), the first product in the nicotinic acid degradation pathway. To understand the mechanism of this regulation, we have determined the crystal structures of BpsR and BpsR in complex with 6HNA. The structures reveal that BpsR binding of 6HNA induces a conformational change in the protein to prevent DNA binding. We have also identified homologs of BpsR in other Gram negative bacteria in which the amino acids involved in recognition of 6HNA are conserved, suggesting a similar mechanism for regulating nicotinic acid degradation.

Structural mechanism for regulation of DNA binding of BpsR, a Bordetella regulator of biofilm formation, by 6-hydroxynicotinic acid.,Booth WT, Davis RR, Deora R, Hollis T PLoS One. 2019 Nov 7;14(11):e0223387. doi: 10.1371/journal.pone.0223387., eCollection 2019. PMID:31697703<ref>PMID:31697703</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6pcp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bordetella pertussis]]
[[Category: Large Structures]]
[[Category: Booth WT]]
[[Category: Davis RR]]
[[Category: Deora R]]
[[Category: Hollis T]]