2RDD
X-ray crystal structure of AcrB in complex with a novel transmembrane helix.
Summary for 2RDD
| Entry DOI | 10.2210/pdb2rdd/pdb |
| Related | 1IWG 1OY8 2DHH 2GIF 2HQC 2J8S |
| Descriptor | Acriflavine resistance protein B, UPF0092 membrane protein yajC, (2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC ACID (3 entities in total) |
| Functional Keywords | drug resistance, multidrug efflux, transporter, antiporter, membrane protein, novel transmembrane helix, acrb, yajc, inner membrane, membrane protein-transport protein complex, membrane protein/transport protein |
| Biological source | Escherichia coli More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P31224 Cell inner membrane; Single-pass membrane protein: P0ADZ7 |
| Total number of polymer chains | 2 |
| Total formula weight | 118811.50 |
| Authors | Tornroth-Horsefield, S.,Gourdon, P.,Horsefield, R.,Neutze, R. (deposition date: 2007-09-22, release date: 2007-12-11, Last modification date: 2023-08-30) |
| Primary citation | Tornroth-Horsefield, S.,Gourdon, P.,Horsefield, R.,Brive, L.,Yamamoto, N.,Mori, H.,Snijder, A.,Neutze, R. Crystal structure of AcrB in complex with a single transmembrane subunit reveals another twist. Structure, 15:1663-1673, 2007 Cited by PubMed Abstract: Bacterial drug resistance is a serious concern for human health. Multidrug efflux pumps export a broad variety of substrates out of the cell and thereby convey resistance to the host. In Escherichia coli, the AcrB:AcrA:TolC efflux complex forms a principal transporter for which structures of the individual component proteins have been determined in isolation. Here, we present the X-ray structure of AcrB in complex with a single transmembrane protein, assigned by mass spectrometry as YajC. A specific rotation of the periplasmic porter domain of AcrB is also revealed, consistent with the hypothesized "twist-to-open" mechanism for TolC activation. Growth experiments with yajc-deleted E. coli reveal a modest increase in the organism's susceptibility to beta-lactam antibiotics, but this effect could not conclusively be attributed to the loss of interactions between YajC and AcrB. PubMed: 18073115DOI: 10.1016/j.str.2007.09.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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