Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex

• Published in: Nature communications Vol. 11; no. 1; p. 4948
• Main Authors: Glavier, Marie, Puvanendran, Dhenesh, Salvador, Dimitri, Decossas, Marion, Phan, Gilles, Garnier, Cyril, Frezza, Elisa, Cece, Quentin, Schoehn, Guy, Picard, Martin, Taveau, Jean-Christophe, Daury, Laetitia, Broutin, Isabelle, Lambert, Olivier
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 02.10.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/326/22/1434; 631/45/535/1258/1259; 631/45/612/1237; 82/80; 82/83; Active transport; Allosteric properties; Antibiotic resistance; Antibiotics; Antiinfectives and antibacterials; Assembly; Cell division; Crystal structure; Drug resistance; E coli; Efflux; Extrusion; Homology; Humanities and Social Sciences; Life Sciences; Lipids; multidisciplinary; Nodulation; Pseudomonas aeruginosa; Science; Science (multidisciplinary); Trimers

The tripartite multidrug efflux system MexAB-OprM is a major actor in Pseudomonas aeruginosa antibiotic resistance by exporting a large variety of antimicrobial compounds. Crystal structures of MexB and of its Escherichia coli homolog AcrB had revealed asymmetric trimers depicting a directional drug...