Homology model of the multidrug transporter LmrA from Lactococcus lactis |
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Authors: | Pleban Karin Macchiarulo Antonio Costantino Gabriele Pellicciari Roberto Chiba Peter Ecker Gerhard F |
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Affiliation: | Department of Pharmaceutical Chemistry, University of Vienna, Althanstrasse 14, A-1090 Wien, Austria. |
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Abstract: | LmrA is an ATP dependent multidrug transporter from Lactococcus lactis conferring antibiotic resistance to 17 out of 21 most frequently administered antibiotics. Starting from the dimeric crystal structure of Vc-MsbA, we built two homology models, with NBD:NBD interfaces reflecting the nonenergized and energized state, respectively. The TMD:TMD topology of the dimer is consistent with the previously obtained substrate photoaffinity labeling pattern suggesting binding of substrates at the TMD:TMD interface involving helix 3 of one monomer and helices 5 and 6 of the other monomer. |
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