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 st ructure and the general tertiary fold of the protein NodF from Rhizobi um leguminosarum. A similarity to acyl carrier proteins of the fatty a cid synthase system had been suggested by the presence of a phosphopan tetheine prosthetic group and a short stretch of sequence homology nea r the prosthetic group attachment site. NMR results suggest that the s tructural homology extends well beyond this region, Both proteins have three well-formed helices which fold in a parallel-antiparallel fashi on and a prosthetic group attachment site near the beginning of the se cond helix.