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5NIL

Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB section

5NIL の概要
エントリーDOI10.2210/pdb5nil/pdb
EMDBエントリー3653
分子名称Outer membrane protein TolC, Macrolide export protein MacA, Macrolide export ATP-binding/permease protein MacB (3 entities in total)
機能のキーワードabc transporter, drug efflux pump, multi-drug resistance, macrolide transporter, toxin transporter, transport protein
由来する生物種Escherichia coli (strain K12)
詳細
タンパク質・核酸の鎖数11
化学式量合計545014.30
構造登録者
主引用文献Fitzpatrick, A.W.P.,Llabres, S.,Neuberger, A.,Blaza, J.N.,Bai, X.C.,Okada, U.,Murakami, S.,van Veen, H.W.,Zachariae, U.,Scheres, S.H.W.,Luisi, B.F.,Du, D.
Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump.
Nat Microbiol, 2:17070-17070, 2017
Cited by
PubMed Abstract: The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.
PubMed: 28504659
DOI: 10.1038/nmicrobiol.2017.70
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (5.3 Å)
構造検証レポート
Validation report summary of 5nil
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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