The glucose transporter of Escherichia coli. Assignment of the 1H, 13C and 15N resonances and identification of the secondary structure of the soluble IIB domain.
The IICBGlc subunit of the Escherichia coli glucose transporter consists of two domains, the membrane-spanning IIC domain, and the hydrophilic IIB domain which contains the phosphorylation site (Cys421). A functional form of the IIB domain was over-expressed separately and isotopically labelled with 13C and 15N. A variety of 15N-edited and 13C, 15N triple-resonance NMR experiments yielded a nearly complete assignment of the 1H, 13C and 15N resonances. Based on the evaluation of conformationally sensitive parameters including NOE effects, scalar couplings and chemical shifts, the secondary structure of the IIB domain is presented. The protein is comprised of four beta-strands forming an antiparallel beta-sheet, two larger alpha-helices at the N- and C-termini and a smaller helical structure of residues 52-58.
Golic Grdadolnik
S
S
Organisch-Chemisches Institut II, Technische Universität München, Garching, Germany.
Eberstadt
M
M
Gemmecker
G
G
Kessler
H
H
Buhr
A
A
Erni
B
B
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D004926:Escherichia coli / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009004:Monosaccharide Transport Proteins / Q000737:chemistry* / Q000235:genetics; D010957:Plasmids; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D000596:Amino Acids; D009004:Monosaccharide Transport Proteins