Rm. Gschwind et al., SECONDARY STRUCTURE OF THE IIB DOMAIN OF THE ESCHERICHIA-COLI MANNOSETRANSPORTER, A NEW FOLD IN THE CLASS OF ALPHA BETA TWISTED OPEN-SHEETSTRUCTURES/, FEBS letters, 404(1), 1997, pp. 45-50
The mannose transporter of the Escherichia coli bacterial phosphotrans
ferase system consists of three subunits: IIAB, IIC and IID. IIAB(Man)
transfers phosphoryl groups to the transported substrate via phosphoh
istidine intermediates. Its IIB domain was overexpressed and isotopica
lly labelled with C-13, N-15 and H-2. Heteronuclear 3D triple-resonanc
e NMR experiments combined with a semi-automatic assignment procedure
yielded the sequential assignment of the H-1, C-13 and N-15 backbone r
esonances. Based on the evaluation of conformationally sensitive param
eters, the secondary structure of the IIBMan domain has been determine
d as an alpha/beta twisted open-sheet structure consisting of a six-st
randed parallel beta-sheet with the novel strand order 3-2-4-1-5-6, si
x helices and a short two-stranded antiparallel beta-sheet. (C) 1997 F
ederation of European Biochemical Societies.