Anthony W P Fitzpatrick / Salomé Llabrés / Arthur Neuberger / James N Blaza / Xiao-Chen Bai / Ui Okada / Satoshi Murakami / Hendrik W van Veen / Ulrich Zachariae / Sjors H W Scheres / Ben F Luisi / Dijun Du /
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 ...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.
EMDB-3653, PDB-5nil: Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB section Method: EM (single particle) / Resolution: 5.3 Å
Source
Escherichia coli K-12 (bacteria)
escherichia coli (strain k12) (bacteria)
Keywords
TRANSPORT PROTEIN / ABC transporter / drug efflux pump / multi-drug resistance / macrolide transporter / toxin transporter
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