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KMID : 0578320190420120850
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Molecules and Cells
2019 Volume.42 No. 12 p.850 ~ p.857
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Crystal Structure of the Regulatory Domain of MexT, a Transcriptional Activator of the MexEFOprN Efflux Pump in Pseudomonas aeruginosa
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Kim Su-Hyeon
Kim Song-Hee H.
Ahn Jin-Sook
Jo In-Seong
Lee Zee-Won
Choi Sang-Ho
Ha Nam-Chul
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Abstract
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The 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.
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KEYWORD
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antibiotic resistance, crystal structure, lysR-type transcriptional regulator, MexT, Pseudomonas aeruginosa
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