Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state
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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 1H, 13C and 15N backbone chemical shift assignments of the isolated 263 amino acid containing NBD of LmrA in its ADP bound state.
KeywordsNMR-assignments Triple resonance experiments ATP binding cassette transporter Nucleotide binding domain Multidrug resistance LmrA
We would like to acknowledge Yalda Shayeghi for initial help with cloning and Nina Christ for purification of TEV protease. This project was supported by the Deutsche Forschungsgemeinschaft (DFG) through the SFB 807 “Transport and communication across biological membranes” (to C.G.), the Center of Excellence Frankfurt (CEF) “Macromolecular complexes”, the Center for Biomolecular Magnetic Resonance Frankfurt (BMRZ) and an Aventis Foundation professorship (to J.W.).
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