4ZJO
Crystal structure of AcrB triple mutant in complex with antibiotic in P21 space group
Summary for 4ZJO
| Entry DOI | 10.2210/pdb4zjo/pdb |
| Descriptor | Multidrug efflux pump subunit AcrB, ERYTHROMYCIN A, DODECYL-BETA-D-MALTOSIDE, ... (4 entities in total) |
| Functional Keywords | transport protein |
| Biological source | Escherichia coli str. K-12 substr. MG1655 |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P31224 |
| Total number of polymer chains | 6 |
| Total formula weight | 686290.15 |
| Authors | Ababou, A.,Koronakis, V. (deposition date: 2015-04-29, release date: 2016-07-27, Last modification date: 2024-01-10) |
| Primary citation | Ababou, A.,Koronakis, V. Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate. Plos One, 11:e0159154-e0159154, 2016 Cited by PubMed Abstract: Gram-negative bacteria such as E. coli use tripartite efflux pumps such as AcrAB-TolC to expel antibiotics and noxious compounds. A key feature of the inner membrane transporter component, AcrB, is a short stretch of residues known as the gate/switch loop that divides the proximal and distal substrate binding pockets. Amino acid substitutions of the gate loop are known to decrease antibiotic resistance conferred by AcrB. Here we present two new AcrB gate loop variants, the first stripped of its bulky side chains, and a second in which the gate loop is removed entirely. By determining the crystal structures of the variant AcrB proteins in the presence and absence of erythromycin and assessing their ability to confer erythromycin tolerance, we demonstrate that the gate loop is important for AcrB export activity but is not required for erythromycin binding. PubMed: 27403665DOI: 10.1371/journal.pone.0159154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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