Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Booth WT, Davis RR, 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. 2019 Nov 7;14(11):e0223387. doi: 10.1371/journal.pone.0223387., eCollection 2019. PMID:31697703 doi:http://dx.doi.org/10.1371/journal.pone.0223387
