Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins.
The structure of a nonspecific lipid transfer protein from barley (ns-LTPbarley) in complex with palmitate has been determined by NMR spectroscopy. The structure has been compared to the structure of ns-LTPbarley in the absence of palmitate, to the structure of ns-LTPbarley in complex with palmitoyl coenzyme A, to the structure of ns-LTPmaize in its free form, and to the maize protein complexed with palmitate. Binding of palmitate only affects the structure of ns-LTPbarley moderately in contrast to the binding of palmitoyl coenzyme A, which leads to a considerable expansion of the protein. The modes of binding palmitate to the maize and barley protein are different. Although in neither case there are major conformational changes in the protein, the orientation of the palmitate in the two proteins is exactly opposite.
Lerche
M H
MH
Carlsberg Laboratorium, Kemisk Afdeling, Valby, Copenhagen, Denmark.
Poulsen
F M
FM
D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D001467:Hordeum / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D019308:Palmitic Acid / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D003313:Zea mays / Q000737:chemistry*
D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant; D019308:Palmitic Acid