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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Fairbrother WJ,Gippert GP,Reizer J,Saier MH Jr,Wright PEdoi
10.1016/0014-5793(92)80367-psubject
Has Abstractpub_date
1992-01-20 00:00:00pages
148-52issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(92)80367-Pjournal_volume
296pub_type
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