6PCO

Mechanism for regulation of DNA binding of Bordetella bronchiseptica BpsR by 6-hydroxynicotinic acid

Summary for 6PCO

• Entry DOI: 10.2210/pdb6pco/pdb
• Related: 6PCP
• Descriptor: MarR-family transcriptional regulator, 1,4-BUTANEDIOL (3 entities in total)
• Functional Keywords: inhibition, biofilm, transcription regulation, bordetella, bpsr, dna binding protein
• Biological source: Bordetella bronchiseptica
• Total number of polymer chains: 4
• Total formula weight: 86960.68

Authors

Booth, W.T.,Davis, R.R.,Deora, R.,Hollis, T. (deposition date: 2019-06-17, release date: 2019-11-06, Last modification date: 2023-10-11)

Primary citation

Booth, W.T.,Davis, R.R.,Deora, R.,Hollis, T.
Structural mechanism for regulation of DNA binding of BpsR, a Bordetella regulator of biofilm formation, by 6-hydroxynicotinic acid.
Plos One, 14:e0223387-e0223387, 2019

PubMed Abstract: 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.

PubMed: 31697703
DOI: 10.1371/journal.pone.0223387

Experimental method

X-RAY DIFFRACTION (2.75 Å)