6Q4N
Fusidic acid bound AcrB_V340A
Summary for 6Q4N
| Entry DOI | 10.2210/pdb6q4n/pdb |
| Descriptor | Multidrug efflux pump subunit AcrB, DECYLAMINE-N,N-DIMETHYL-N-OXIDE, HEXANE, ... (15 entities in total) |
| Functional Keywords | multidrug efflux protein, membrane protein, transport protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 5 |
| Total formula weight | 392786.61 |
| Authors | |
| Primary citation | Tam, H.K.,Malviya, V.N.,Foong, W.E.,Herrmann, A.,Malloci, G.,Ruggerone, P.,Vargiu, A.V.,Pos, K.M. Binding and Transport of Carboxylated Drugs by the Multidrug Transporter AcrB. J.Mol.Biol., 432:861-877, 2020 Cited by PubMed Abstract: AcrAB(Z)-TolC is the main drug efflux transporter complex in Escherichia coli. The extrusion of various toxic compounds depends on several drug binding sites within the trimeric AcrB transporter. Membrane-localized carboxylated substrates, such as fusidic acid and hydrophobic β-lactams, access the pump via a groove between the transmembrane helices TM1 and TM2. In this article, the transport route from the initial TM1/TM2 groove binding site toward the deep binding pocket located in the periplasmic part has been addressed via molecular modeling studies followed by functional and structural characterization of several AcrB variants. We propose that membrane-embedded drugs bind initially to the TM1/TM2 groove, are oriented by the AcrB PN2 subdomain, and are subsequently transported via a PN2/PC1 interface pathway directly toward the deep binding pocket. Our work emphasizes the exploitation of multiple transport pathways by AcrB tuned to substrate physicochemical properties related to the polyspecificity of the pump. PubMed: 31881208DOI: 10.1016/j.jmb.2019.12.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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