1BE2

LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES

Summary for 1BE2

• Entry DOI: 10.2210/pdb1be2/pdb
• Descriptor: LIPID TRANSFER PROTEIN, PALMITIC ACID (2 entities in total)
• Functional Keywords: lipid transport, lipid transfer protein, palmitate
• Biological source: Hordeum vulgare
• Total number of polymer chains: 1
• Total formula weight: 9961.39

Authors

Lerche, M.H.,Poulsen, F.M. (deposition date: 1998-05-19, release date: 1998-12-02, Last modification date: 2024-11-20)

Primary citation

Lerche, M.H.,Poulsen, F.M.
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.
Protein Sci., 7:2490-2498, 1998

PubMed 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.

PubMed: 9865943

Experimental method

SOLUTION NMR