5XQL

Crystal structure of a Pseudomonas aeruginosa transcriptional regulator

Summary for 5XQL

• Entry DOI: 10.2210/pdb5xql/pdb
• Descriptor: Multidrug-efflux transporter 1 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) (2 entities in total)
• Functional Keywords: pseudomonas aeruginosa, transcriptional regulator, transcription
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 34820.57

Authors

Raju, H.,Sharma, R. (deposition date: 2017-06-07, release date: 2017-06-28, Last modification date: 2024-03-27)

Primary citation

Raju, H.,Sharma, R.
Crystal structure of BrlR with c-di-GMP
Biochem. Biophys. Res. Commun., 490:260-264, 2017

PubMed Abstract: The transcriptional regulator BrlR is a member of the MerR family of multidrug transport activators in Pseudomonas aeruginosa. Recent study indicates that BrlR is a novel 3',5'-cyclic diguanylic acid (c-di-GMP) receptor and can be activated by c-di-GMP. To gain insight into BrlR function, we determined the structure of BrlR with c-di-GMP complex structure to 2.5 Å. The structure and size exclusion chromatography (SEC) data revealed BrlR forms a tetramer and each BrlR protomer consists of three parts, DNA-binding domain, a coiled-coil region and GyrI-like domain. There are two different c-di-GMP binding sites located mainly at the DNA binding domain of each BrlR protomer and do not overlap with the GyrI-like domain. The drug-binding pocket in GyrI-like domain is much conserved indicating it can also bind flat-shaped molecules like other multidrug resistance (MDR) proteins.

PubMed: 28619510
DOI: 10.1016/j.bbrc.2017.06.033

Experimental method

X-RAY DIFFRACTION (2.494 Å)