6SGU
Cryo-EM structure of Escherichia coli AcrB and DARPin in Saposin A-nanodisc
Summary for 6SGU
| Entry DOI | 10.2210/pdb6sgu/pdb |
| EMDB information | 10185 |
| Descriptor | Multidrug efflux pump subunit AcrB, DARPin (2 entities in total) |
| Functional Keywords | rnd transporter, efflux pump, drug transport, antibiotic resistance, lipid nanodisc, membrane protein |
| Biological source | Escherichia coli K12 More |
| Total number of polymer chains | 5 |
| Total formula weight | 377630.67 |
| Authors | Szewczak-Harris, A.,Du, D.,Newman, C.,Neuberger, A.,Luisi, B.F. (deposition date: 2019-08-05, release date: 2020-05-13, Last modification date: 2024-05-22) |
| Primary citation | Du, D.,Neuberger, A.,Orr, M.W.,Newman, C.E.,Hsu, P.C.,Samsudin, F.,Szewczak-Harris, A.,Ramos, L.M.,Debela, M.,Khalid, S.,Storz, G.,Luisi, B.F. Interactions of a Bacterial RND Transporter with a Transmembrane Small Protein in a Lipid Environment. Structure, 28:625-, 2020 Cited by PubMed Abstract: The small protein AcrZ in Escherichia coli interacts with the transmembrane portion of the multidrug efflux pump AcrB and increases resistance of the bacterium to a subset of the antibiotic substrates of that transporter. It is not clear how the physical association of the two proteins selectively changes activity of the pump for defined substrates. Here, we report cryo-EM structures of AcrB and the AcrBZ complex in lipid environments, and comparisons suggest that conformational changes occur in the drug-binding pocket as a result of AcrZ binding. Simulations indicate that cardiolipin preferentially interacts with the AcrBZ complex, due to increased contact surface, and we observe that chloramphenicol sensitivity of bacteria lacking AcrZ is exacerbated when combined with cardiolipin deficiency. Taken together, the data suggest that AcrZ and lipid cooperate to allosterically modulate AcrB activity. This mode of regulation by a small protein and lipid may occur for other membrane proteins. PubMed: 32348749DOI: 10.1016/j.str.2020.03.013 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.27 Å) |
Structure validation
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