title: Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three-dimensional NMR spectroscopy.
abstract: A low resolution solution structure of the IIA domain of the Bacillus subtilis phosphoenolpyruvate-sugar phosphotransferase system (PTS) glucose permease has been determined using 945 inter-residue and 724 intra-residue distance constraints derived from three-dimensional 15N and 13C edited NOESY spectra. A total of 15 structures was generated using distance geometry calculations. The protein is comprised of 13 beta-strands forming an antiparallel beta-barrel. The average backbone atomic RMS deviation about the average distance geometry structure for the beta-sheet residues is 1.1 A. The conformations of the loop regions between the beta-strands are less well determined. Backbone distance constraints obtained during the process of sequential assignment were insufficient to correctly calculate the polypeptide fold.
authors.affiliation: Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
authors.forename: W J
authors.initials: WJ
authors.lastname: Fairbrother
authors.forename: G P
authors.initials: GP
authors.lastname: Gippert
authors.forename: J
authors.initials: J
authors.lastname: Reizer
authors.forename: M H
authors.initials: MH
authors.lastname: Saier
authors.forename: P E
authors.initials: PE
authors.lastname: Wright
mesh_terms: D001412:Bacillus subtilis / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D009587:Nitrogen Isotopes; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase