NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein.
Heteronuclear NMR methods have been used to elucidate the secondary structure and the general tertiary fold of the protein NodF from Rhizobium leguminosarum. A similarity to acyl carrier proteins of the fatty acid synthase system had been suggested by the presence of a phosphopantetheine prosthetic group and a short stretch of sequence homology near the prosthetic group attachment site. NMR results suggest that the structural homology extends well beyond this region. Both proteins have three well-formed helices which fold in a parallel-antiparallel fashion and a prosthetic group attachment site near the beginning of the second helix.
Ghose
R
R
Department of Chemistry, Yale University, New Haven, CT 06520, USA.
Geiger
O
O
Prestegard
J H
JH
D000213:Acyl Carrier Protein / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D004926:Escherichia coli / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010204:Pantetheine / Q000031:analogs & derivatives / Q000737:chemistry; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016961:Rhizobium leguminosarum / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; C068605:nodF protein, Rhizobium; D010204:Pantetheine; C003129:4'-phosphopantetheine