title: Homology model of the multidrug transporter LmrA from Lactococcus lactis.
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.
authors.affiliation: Department of Pharmaceutical Chemistry, University of Vienna, Althanstrasse 14, A-1090 Wien, Austria.
authors.forename: Karin
authors.initials: K
authors.lastname: Pleban
authors.forename: Antonio
authors.initials: A
authors.lastname: Macchiarulo
authors.forename: Gabriele
authors.initials: G
authors.lastname: Costantino
authors.forename: Roberto
authors.initials: R
authors.lastname: Pellicciari
authors.forename: Peter
authors.initials: P
authors.lastname: Chiba
authors.forename: Gerhard F
authors.initials: GF
authors.lastname: Ecker
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D018432:Drug Resistance, Multiple; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry*; D040681:Structural Homology, Protein
chemical_list: D001426:Bacterial Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C101824:LmrA protein, Lactococcus lactis