5XBT

The structure of BrlR bound to c-di-GMP

Summary for 5XBT

• Entry DOI: 10.2210/pdb5xbt/pdb
• Related: 5XBW
• Descriptor: Probable transcriptional regulator, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), GLYCEROL, ... (6 entities in total)
• Functional Keywords: c-di-gmp, receptor, hth domain, dna binding protein
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 2
• Total formula weight: 66523.76

Authors

Wang, F.,Qing, H.,Gu, L. (deposition date: 2017-03-21, release date: 2018-05-02, 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 (2.495 Å)