Literature DB >> 15501048

Homology model of the multidrug transporter LmrA from Lactococcus lactis.

Karin Pleban1, Antonio Macchiarulo, Gabriele Costantino, Roberto Pellicciari, Peter Chiba, Gerhard F Ecker.   

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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Year:  2004        PMID: 15501048     DOI: 10.1016/j.bmcl.2004.09.040

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  1 in total

1.  Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism.

Authors:  Hiroshi Omote; Marwan K Al-Shawi
Journal:  Biophys J       Date:  2006-03-24       Impact factor: 4.033

  1 in total

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