Reference "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"

Reference ID

8710

Title

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

Source

Protein science : a publication of the Protein Society, 1998, vol. 7, pp. 2490-2498

Authors (2)

Lerche-M-H

Poulsen-F-M

Abstract

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.