NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein

FEBS Lett. 1996 Jun 10;388(1):66-72. doi: 10.1016/0014-5793(96)00512-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyl Carrier Protein / chemistry*
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Escherichia coli / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Pantetheine / analogs & derivatives
  • Pantetheine / chemistry
  • Protein Folding
  • Protein Structure, Secondary
  • Rhizobium leguminosarum / chemistry*
  • Sequence Homology, Amino Acid*


  • Acyl Carrier Protein
  • Bacterial Proteins
  • nodF protein, Rhizobium
  • Pantetheine
  • 4'-phosphopantetheine