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Crystal structure of the regulatory domain of MexT, a transcriptional activator in Pseudomonas aeruginosaCrystal structure of the regulatory domain of MexT, a transcriptional activator in Pseudomonas aeruginosa
Structural highlights
FunctionPublication Abstract from PubMedThe Gram-negative opportunistic pathogen, Pseudomonas aeruginosa, has multiple multidrug efflux pumps. MexT, a LysR-type transcriptional regulator, functions as a transcriptional activator of the MexEF-OprN efflux system. MexT consists of an N-terminal DNA-binding domain and a C-terminal regulatory domain (RD). Little is known regarding MexT ligands and its mechanism of activation. We elucidated the crystal structure of the MexT RD at 2.0 A resolution. The structure comprised two protomer chains in a dimeric arrangement. MexT possessed an arginine-rich region and a hydrophobic patch lined by a variable loop, both of which are putative ligand-binding sites. The three-dimensional structure of MexT provided clues to the interacting ligand structure. A DNase I footprinting assay of full-length MexT identified two MexT-binding sequence in the mexEF-oprN promoter. Our findings enhance the understanding of the regulation of MexT-dependent activation of efflux pumps. Crystal Structure of the Regulatory Domain of MexT, a Transcriptional Activator of the MexEFOprN Efflux Pump in Pseudomonas aeruginosa.,Kim S, Kim SH, Ahn J, Jo I, Lee ZW, Choi SH, Ha N Mol Cells. 2019 Nov 14. pii: molcells.2019.0168. doi:, 10.14348/molcells.2019.0168. PMID:31722511[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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