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Article Dans Une Revue Biochimica et Biophysica Acta:Biomembranes Année : 2021

Structural characterization of the EmrAB-TolC efflux complex from E. coli

Résumé

Gram-negative bacteria export a large variety of antimicrobial compounds by forming two-membrane spanning tripartite multidrug efflux systems composed of an inner membrane transporter, an outer membrane channel and a periplasmic adaptor protein. Here we present the co-expression, purification and first electron microscopy insights of the Escherichia coli EmrAB-TolC tripartite Major Facilitator Superfamily (MSF) efflux system as a whole complex stabilized by Amphipol polymer. The structure reveals a 33 nm long complex delineated by the Amphipol belt at both extremities. Comparison of projection structures of EmrAB-TolC and AcrAB-TolC indicates that the outer membrane protein TolC linked to the periplasmic adaptor EmrA protein form an extended periplasmic canal. The overall length of EmrAB-TolC complex is similar to that of AcrAB-TolC with a probable tip-to-tip interaction between EmrA and TolC unveiling how the adaptor protein connects TolC and EmrB embedded in the inner membrane.
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Dates et versions

hal-03440986 , version 1 (22-11-2021)

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Narek Yousefian, Alina Ornik-Cha, Sylvie Poussard, Marion Decossas, Melanie Berbon, et al.. Structural characterization of the EmrAB-TolC efflux complex from E. coli. Biochimica et Biophysica Acta:Biomembranes, 2021, 1863 (1), pp.183488. ⟨10.1016/j.bbamem.2020.183488⟩. ⟨hal-03440986⟩

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