PMID:9688273
| Citation |
Schwaiger, M, Lebendiker, M, Yerushalmi, H, Coles, M, Gröger, A, Schwarz, C, Schuldiner, S and Kessler, H (1998) NMR investigation of the multidrug transporter EmrE, an integral membrane protein. Eur. J. Biochem. 254:610-9 |
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| Abstract |
EmrE is an Escherichia coli multidrug transport protein that confers resistance to a wide range of toxicants by active transport across the bacterial cell membrane. The highly hydrophobic polytopic integral membrane protein has been purified and studied in its full-length form by high-resolution NMR spectroscopy in a mixture of chloroform/methanol/water (6:6:1, by vol.). Full activity is maintained after reconstitution of the protein into proteoliposomes from this solvent mixture. A series of heteronuclear (1H-15N) two- and three-dimensional experiments, as well as triple resonance experiments, were applied to the 110-residue protein and led to the assignment of the 1H, 15N and a large part of the 13C backbone resonances as well as many of the sidechain resonances. A preliminary analysis of the secondary structure, based on sequential NOE connectivities, deviation of chemical shifts from random coil values and 3J(NH-H alpha) coupling constants supports a model where the protein forms four alpha-helices between residues 4-26 (TM1), 32-53 (TM2), 58-76 (TM3) and 85-106 (TM4). For the residues of helices TM2 and TM3 a significant line broadening occurs due to slow conformational processes. |
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| Keywords |
Amino Acid Sequence; Antiporters; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Carrier Proteins/chemistry; Carrier Proteins/isolation & purification; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli Proteins; Magnetic Resonance Spectroscopy; Membrane Proteins/chemistry; Membrane Proteins/isolation & purification; Molecular Sequence Data; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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