title: NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein.
abstract: 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.
authors.affiliation: Department of Chemistry, Yale University, New Haven, CT 06520, USA.
authors.forename: R
authors.initials: R
authors.lastname: Ghose
authors.forename: O
authors.initials: O
authors.lastname: Geiger
authors.forename: J H
authors.initials: JH
authors.lastname: Prestegard
mesh_terms: 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
chemical_list: D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; C068605:nodF protein, Rhizobium; D010204:Pantetheine; C003129:4'-phosphopantetheine