Journal
NATURE MICROBIOLOGY
Volume 2, Issue 7, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nmicrobiol.2017.70
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Funding
- Wellcome Trust
- Human Frontiers Science Program
- Marie Curie International Outgoing Fellowship
- UK Medical Research Council [MC_UP_A025_1013]
- Wellcome Trust ISSF award [WT097818MF]
- Scottish Universities' Physics Alliance
- MRC Mitochondrial Biology Unit [U105663141]
- Herchel-Smith Scholarship
- BBSRC [BB/K017713/1, BB/R00224X/1] Funding Source: UKRI
- MRC [MC_UP_A025_1013, MC_PC_14116] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/R00224X/1, BB/K017713/1] Funding Source: researchfish
- Medical Research Council [MC_UP_A025_1013, MC_PC_14116] Funding Source: researchfish
- Direct For Biological Sciences
- Div Of Biological Infrastructure [1338135] Funding Source: National Science Foundation
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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 cryomicroscopy 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.
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