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    FEBS Lett. 1997 Mar 3;404(1):45-50.

    Secondary structure of the IIB domain of the Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures.

    Gschwind RM, Gemmecker G, Leutner M, Kessler H, Gutknecht R, Lanz R, Flükiger K, Erni B.

    Institut für Organische Chemie und Biochemie II, Technische Universität München, Germany.

    The mannose transporter of the Escherichia coli bacterial phosphotransferase system consists of three subunits: IIAB, IIC and IID. IIABMan transfers phosphoryl groups to the transported substrate via phosphohistidine intermediates. Its IIB domain was overexpressed and isotopically labelled with 13C, 15N and 2H. Heteronuclear 3D triple-resonance NMR experiments combined with a semi-automatic assignment procedure yielded the sequential assignment of the 1H, 13C and 15N backbone resonances. Based on the evaluation of conformationally sensitive parameters, the secondary structure of the IIBMan domain has been determined as an alpha/beta twisted open-sheet structure consisting of a six-stranded parallel beta-sheet with the novel strand order 3-2-4-1-5-6, six helices and a short two-stranded antiparallel beta-sheet.

    PMID: 9074635 [PubMed - indexed for MEDLINE]

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