1bwo
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(New page: 200px<br /><applet load="1bwo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bwo, resolution 2.10Å" /> '''THE CRYSTAL STRUCTUR...)
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Revision as of 09:51, 20 November 2007
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THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION
Overview
Nonspecific lipid transfer proteins (ns-LTP1) form a multigenic protein, family in plants. In vitro they are able to bind all sort of lipids but, their function, in vivo, remains speculative. A ns-LTP1 isolated from, wheat seed was crystallized in the presence of, lyso-myristoyl-phosphatidylcholine (LMPC). The structure was solved by, molecular replacement and refined to 2.1 A resolution to an R-factor of, 16.3% and a free R-factor of 21.3%. It reveals for the first time that the, protein binds two LMPC molecules that are inserted head to tail in a, hydrophobic cavity. A detailed study of the structure leads to the, conclusion that there are two lipid-binding sites, one of which shows a, higher affinity for the LMPC than the other. Comparison with other, structures of lipid-bound ns-LTP1 suggests that the presence of two, binding sites is a general feature of plant ns-LTP1.
About this Structure
1BWO is a Single protein structure of sequence from Triticum aestivum with LPC as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 A resolution., Charvolin D, Douliez JP, Marion D, Cohen-Addad C, Pebay-Peyroula E, Eur J Biochem. 1999 Sep;264(2):562-8. PMID:10491104
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