title: Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state.
abstract: LmrA from Lactococcus lactis is a multidrug transporter and a member of the ATP binding cassette (ABC) transporter family. ABC transporters consist of a transmembrane domain (TMD) and a nucleotide binding domain (NBD). The NBD contains the highly conserved signature motifs of this transporter superfamily. In the case of LmrA, the TMD and the NBD are expressed as a single polypeptide. LmrA catalyzes the extrusion of hydrophobic compounds including antibiotics from the cell membrane at the expense of ATP hydrolysis. ATP binds to the NBD, where binding and hydrolysis induce conformational changes that lead to the extrusion of the substrate via the TMD. Here, we report the (1)H, (13)C and (15)N backbone chemical shift assignments of the isolated 263 amino acid containing NBD of LmrA in its ADP bound state.
authors.affiliation: Institut für Molekulare Biowissenschaften, Johann-Wolfgang-Goethe-Universität Frankfurt/M., Max-von-Laue-Str. 9, 60438 Frankfurt, Germany.
authors.forename: Ute A
authors.initials: UA
authors.lastname: Hellmich
authors.forename: Elke
authors.initials: E
authors.lastname: Duchardt-Ferner
authors.forename: Clemens
authors.initials: C
authors.lastname: Glaubitz
authors.forename: Jens
authors.initials: J
authors.lastname: Wöhnert
mesh_terms: D000244:Adenosine Diphosphate / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D013294:Lactococcus lactis; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry* / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D000244:Adenosine Diphosphate; D001426:Bacterial Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C101824:LmrA protein, Lactococcus lactis