Low resolution solution structure of the Bacillus subtilis glucose permease IIA domain derived from heteronuclear three‐dimensional NMR spectroscopy

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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 β-strands forming an antiparallel β-barrel, The average backbone atomic RMS deviation about the average distance geometry structure for the β-sheet residues is 1.1 Å. The conformations of the loop regions between the β-strands are less well determined. Backbone distance constraints obtained during the process of sequential assignment were insufficient to correctly calculate the polypeptide fold.

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