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Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB sectionStructure of the MacAB-TolC ABC-type tripartite multidrug efflux pump-MacB section
Structural highlights
FunctionTOLC_ECOLI Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe 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. Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump.,Fitzpatrick AWP, Llabres S, Neuberger A, Blaza JN, Bai XC, Okada U, Murakami S, van Veen HW, Zachariae U, Scheres SHW, Luisi BF, Du D Nat Microbiol. 2017 May 15;2:17070. doi: 10.1038/nmicrobiol.2017.70. PMID:28504659[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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