PMID:15111118
| Citation |
Pos, KM, Schiefner, A, Seeger, MA and Diederichs, K (2004) Crystallographic analysis of AcrB. FEBS Lett. 564:333-9 |
|---|---|
| Abstract |
A His-tagged derivative of the multidrug efflux pump AcrB could be crystallized in three different space groups (R3, R32 and P321). Experimental MAD-phasing maps from R32 AcrB(His) crystals were obtained to a resolution of 3.5 A. Datasets of native and substrate soaked AcrB(His) crystals were collected at the Swiss Light Source X06SA beamline up to a resolution of 2.7 A and refinement of these data provided good quality electron density maps, which allowed us to complement the published AcrB structure (PDB code 1iwg). Introduction of amino acids 860-865 and 868 lacking in the 1iwg structure and deletion of a highly disordered region (amino acids 669-678) improved R(free) and average B factors in the 2.7 A model. We could not identify significant densities indicating specific antibiotic binding sites in the AcrB R32 space group datasets under the soaking conditions tested. |
| Links |
PubMed Online version:10.1016/S0014-5793(04)00272-8 |
| Keywords |
Carrier Proteins/chemistry; Carrier Proteins/genetics; Crystallography, X-Ray; Drug Resistance, Multiple, Bacterial; Escherichia coli/chemistry; Escherichia coli/drug effects; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Membrane Proteins/chemistry; Membrane Proteins/genetics; Models, Molecular; Molecular Structure; Multidrug Resistance-Associated Proteins; Protein Binding; Protein Structure, Quaternary |
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