NMR INVESTIGATIONS OF THE STRUCTURAL-PROPERTIES OF THE NODULATION PROTEIN, NODF, FROM RHIZOBIUM-LEGUMINOSARUM AND ITS HOMOLOGY WITH ESCHERICHIA-COLI ACYL CARRIER PROTEIN
R. Ghose et al., NMR INVESTIGATIONS OF THE STRUCTURAL-PROPERTIES OF THE NODULATION PROTEIN, NODF, FROM RHIZOBIUM-LEGUMINOSARUM AND ITS HOMOLOGY WITH ESCHERICHIA-COLI ACYL CARRIER PROTEIN, FEBS letters, 388(1), 1996, pp. 66-72
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.