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

Ruth M. Gschwind, Gerd Gemmecker, Michael Leutner, Horst Kessler, Regula Gutknecht, Regina Lanz, Karin Flükiger, Bernhard Erni

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The mannose transporter of the Escherichia coli bacterial phosphotransferase system consists of three subunits: IIAB, IIC and IID. IIAB(Man) 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 IIB(Man) 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.

Original languageEnglish
Pages (from-to)45-50
Number of pages6
JournalFEBS Letters
Volume404
Issue number1
DOIs
StatePublished - 3 Mar 1997

Keywords

  • Bacterial phosphotransferase system
  • Escherichia coli
  • Heteronuclear NMR
  • Histidine phosphate
  • Secondary structure

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