1H and 15N resonance assignments and structure of the N-terminal domain of Escherichia coli initiation factor 3.
Initiation factor IF3 from Escherichia coli is composed of two domains connected by a hydrophilic peptide. In this study, the N-terminal domain (residues 7-83) has been overexpressed, 15N labelled and purified. NMR assignments for this domain have been obtained by two-dimensional and three-dimensional heteronuclear and homonuclear spectroscopy. Using distance geometry and simulated annealing, a three-dimensional solution structure was calculated using 506 NOE and 56 dihedral angle restraints. The resulting structure is composed of a five-stranded antiparallel beta sheet surrounded by two alpha helices. Since the heteronuclear 1H-15N correlation spectrum of the N-terminal domain of IF3 is an almost exact subset of that of the native protein, the assignments obtained and the structure calculated should be directly transposable to the full-length protein.
Garcia
C
C
Laboratoire de synthèse organique, URA 1308 du CNRS, Ecole Polytechnique, Palaiseau, France.
Fortier
P L
PL
Blanquet
S
S
Lallemand
J Y
JY
Dardel
F
F
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010448:Peptide Initiation Factors / Q000737:chemistry*; D039665:Prokaryotic Initiation Factor-3; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D010448:Peptide Initiation Factors; D039665:Prokaryotic Initiation Factor-3