6T7S

MexB structure solved by cryo-EM in nanodisc in absence of its protein partners

6T7S の概要

• エントリーDOI: 10.2210/pdb6t7s/pdb
• 関連するPDBエントリー: 6TA5 6TA6
• EMDBエントリー: 10371
• 分子名称: Efflux pump membrane transporter (1 entity in total)
• 機能のキーワード: transporter, efflux, proton motive force, bacterial resistance, antimicrobial protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 341118.02

構造登録者

Glavier, M.,Schoehn, G.,Taveau, J.C.,Phan, G.,Daury, L.,Lambert, O.,Broutin, I. (登録日: 2019-10-23, 公開日: 2020-09-16, 最終更新日: 2024-05-15)

主引用文献

Glavier, M.,Puvanendran, D.,Salvador, D.,Decossas, M.,Phan, G.,Garnier, C.,Frezza, E.,Cece, Q.,Schoehn, G.,Picard, M.,Taveau, J.C.,Daury, L.,Broutin, I.,Lambert, O.
Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex.
Nat Commun, 11:4948-4948, 2020

PubMed Abstract: 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 pathway by a conformational interconversion (from Loose and Tight binding pockets to Open gate (LTO) for drug exit). It remains unclear how MexB acquires its LTO form. Here by performing functional and cryo-EM structural investigations of MexB at various stages of the assembly process, we unveil that MexB inserted in lipid membrane is not set for active transport because it displays an inactive LTC form with a Closed exit gate. In the tripartite complex, OprM and MexA form a corset-like platform that converts MexB into the active form. Our findings shed new light on the resistance nodulation cell division (RND) cognate partners which act as allosteric factors eliciting the functional drug extrusion.

PubMed: 33009415
DOI: 10.1038/s41467-020-18770-5

実験手法

ELECTRON MICROSCOPY (4.5 Å)