Gschwind, R. M. and Gemmecker, G. and Leutner, M. and Kessler, H. and Gutknecht, R. and Lanz, R. and Flückiger, K. and Erni, B. (1997) Secondary structure of the IIB domain of Escherichia coli mannose transporter, a new fold in the class of alpha/beta twisted open-sheet structures. FEBS Letters 404 (1), pp. 45-50.
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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 α/β twisted open-sheet structure consisting of a six-stranded parallel β-sheet with the novel strand order 3–2–4–1–5–6, six helices and a short two-stranded antiparallel β-sheet.
|Institutions:||Chemistry and Pharmacy > Institut für Organische Chemie > Arbeitskreis Prof. Dr. Ruth Gschwind|
|Keywords:||Bacterial phosphotransferase system; Heteronuclear NMR; Secondary structure; Histidine phosphate; (Escherichia coli)|
|Subjects:||500 Science > 570 Life sciences|
500 Science > 540 Chemistry & allied sciences
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||No|
|Deposited On:||10 Nov 2009 16:49|
|Last Modified:||10 Nov 2009 16:49|
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