31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE. Export

@article{citeulike:1666030, abstract = {The binding of tetraphenylphosphonium (TPP+) to EmrE, a membrane-bound, 110 residue Escherichia coli multidrug transport protein, has been observed by 31P cross-polarisation-magic-angle spinning nuclear magnetic resonance spectroscopy (CP-MAS NMR). EmrE has been reconstituted into dimyristoyl phosphatidylcholine bilayers. CP-MAS could selectively distinguish binding of TPP+ to EmrE in the fluid membrane. A population of bound ligand appears shifted 4 ppm to lower frequency compared to free ligand in solution, which suggests a rather direct and specific type of interaction of the ligand with the protein. This is also supported by the observed restricted motion of the bound ligand. The observation of another weakly bound substrate population arises from ligand binding to negatively charged residues in the protein loop regions.}, address = {Department of Biochemistry, University of Oxford, UK. glaubitz@bioch.ox.ac.uk}, author = {Glaubitz, C. and Groeger, A. and Gottschalk, K. and Spooner, P. and Watts, A. and Schuldiner, S. and Kessler, H.}, citeulike-article-id = {1666030}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11034313}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11034313}, day = {1}, issn = {0014-5793}, journal = {FEBS Lett}, keywords = {31p, emre, mas, ssnmr}, month = {September}, number = {2-3}, pages = {127--131}, posted-at = {2008-07-22 15:11:28}, priority = {2}, title = {31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11034313}, volume = {480}, year = {2000} }

TY - JOUR ID - citeulike:1666030 L3 - citeulike-article-id:1666030 N2 - The binding of tetraphenylphosphonium (TPP+) to EmrE, a membrane-bound, 110 residue Escherichia coli multidrug transport protein, has been observed by 31P cross-polarisation-magic-angle spinning nuclear magnetic resonance spectroscopy (CP-MAS NMR). EmrE has been reconstituted into dimyristoyl phosphatidylcholine bilayers. CP-MAS could selectively distinguish binding of TPP+ to EmrE in the fluid membrane. A population of bound ligand appears shifted 4 ppm to lower frequency compared to free ligand in solution, which suggests a rather direct and specific type of interaction of the ligand with the protein. This is also supported by the observed restricted motion of the bound ligand. The observation of another weakly bound substrate population arises from ligand binding to negatively charged residues in the protein loop regions. IS - 2-3 JF - FEBS Lett SN - 0014-5793 AD - Department of Biochemistry, University of Oxford, UK. glaubitz@bioch.ox.ac.uk EP - 131 TI - 31P-CP-MAS NMR studies on TPP+ bound to the ion-coupled multidrug transport protein EmrE. VL - 480 SP - 127 KW - 31p KW - emre KW - mas KW - ssnmr AU - Glaubitz, C AU - Groeger, A AU - Gottschalk, K AU - Spooner, P AU - Watts, A AU - Schuldiner, S AU - Kessler, H PY - 2000/09/01/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11034313 ER -