1be2
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(New page: 200px<br /> <applet load="1be2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1be2" /> '''LIPID TRANSFER PROTEIN COMPLEXED WITH PALMI...)
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Revision as of 18:53, 29 October 2007
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LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES
Overview
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 ... [(full description)]
About this Structure
1BE2 is a [Single protein] structure of sequence from [Hordeum vulgare] with PLM as [ligand]. Full crystallographic information is available from [OCA].
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., Lerche MH, Poulsen FM, Protein Sci. 1998 Dec;7(12):2490-8. PMID:9865943
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