Protein Science, Vol 7, Issue 12 2490-2498, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

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

M. H. LERCHE and F. M. POULSEN
Carlsberg Laboratorium, Kemisk Afdeling, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark

The structure of a nonspecific lipid transfer protein from barley (ns-LTP(barley)) in complex with palmitate has been determined by NMR spectroscopy. The structure has been compared to the structure of ns-LTP(barley) in the absence of palmitate, to the structure of ns-LTP(barley) in complex with palmitoyl coenzyme A, to the structure of ns-LTP(maize) in its free form, and to the maize protein complexed with palmitate. Binding of palmitate only affects the structure of ns-LTP(barley) 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.
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