5JMN
Fusidic acid bound AcrB
Summary for 5JMN
| Entry DOI | 10.2210/pdb5jmn/pdb |
| Descriptor | Multidrug efflux pump subunit AcrB, DODECANE, N-OCTANE, ... (14 entities in total) |
| Functional Keywords | multidrug efflux protein, membrane protein, transport protein |
| Biological source | Escherichia coli (strain K12) More |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P31224 |
| Total number of polymer chains | 5 |
| Total formula weight | 393607.11 |
| Authors | Oswald, C.,Tam, H.K.,Pos, K.M. (deposition date: 2016-04-29, release date: 2016-12-21, Last modification date: 2024-01-10) |
| Primary citation | Oswald, C.,Tam, H.K.,Pos, K.M. Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB. Nat Commun, 7:13819-13819, 2016 Cited by PubMed Abstract: The deployment of multidrug efflux pumps is a powerful defence mechanism for Gram-negative bacterial cells when exposed to antimicrobial agents. The major multidrug efflux transport system in Escherichia coli, AcrAB-TolC, is a tripartite system using the proton-motive force as an energy source. The polyspecific substrate-binding module AcrB uses various pathways to sequester drugs from the periplasm and outer leaflet of the inner membrane. Here we report the asymmetric AcrB structure in complex with fusidic acid at a resolution of 2.5 Å and mutational analysis of the putative fusidic acid binding site at the transmembrane domain. A groove shaped by the interface between transmembrane helix 1 (TM1) and TM2 specifically binds fusidic acid and other lipophilic carboxylated drugs. We propose that these bound drugs are actively displaced by an upward movement of TM2 towards the AcrB periplasmic porter domain in response to protonation events in the transmembrane domain. PubMed: 27982032DOI: 10.1038/ncomms13819 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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