5XBI

The structure of BrlR-C domain bound to 3-amino-2-phenazino(a pyocyanin analog)

Summary for 5XBI

• Entry DOI: 10.2210/pdb5xbi/pdb
• Descriptor: Probable transcriptional regulator, 3-azanylphenazin-2-ol, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: gyri-like domain, receptor, pyocyanin analog, transcription
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 35195.31

Authors

Wang, F.,Qing, H.,Gu, L. (deposition date: 2017-03-17, release date: 2018-03-21, Last modification date: 2024-03-27)

Primary citation

Wang, F.,He, Q.,Yin, J.,Xu, S.,Hu, W.,Gu, L.
BrlR from Pseudomonas aeruginosa is a receptor for both cyclic di-GMP and pyocyanin.
Nat Commun, 9:2563-2563, 2018

PubMed Abstract: The virulence factor pyocyanin and the intracellular second messenger cyclic diguanylate monophosphate (c-di-GMP) play key roles in regulating biofilm formation and multi-drug efflux pump expression in Pseudomonas aeruginosa. However, the crosstalk between these two signaling pathways remains unclear. Here we show that BrlR (PA4878), previously identified as a c-di-GMP responsive transcriptional regulator, acts also as a receptor for pyocyanin. Crystal structures of free BrlR and c-di-GMP-bound BrlR reveal that the DNA-binding domain of BrlR contains two separate c-di-GMP binding sites, both of which are involved in promoting brlR expression. In addition, we identify a pyocyanin-binding site on the C-terminal multidrug-binding domain based on the structure of the BrlR-C domain in complex with a pyocyanin analog. Biochemical analysis indicates that pyocyanin enhances BrlR-DNA binding and brlR expression in a concentration-dependent manner.

PubMed: 29967320
DOI: 10.1038/s41467-018-05004-y

Experimental method

X-RAY DIFFRACTION (1.4 Å)