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New page: left|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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[[Image:1bwo.jpg|left|200px]]<br /><applet load="1bwo" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bwo.jpg|left|200px]]<br /><applet load="1bwo" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bwo, resolution 2.10&Aring;" />
caption="1bwo, resolution 2.10&Aring;" />
'''THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION'''<br />
'''THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1BWO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with LPC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BWO OCA].  
1BWO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum] with <scene name='pdbligand=LPC:'>LPC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWO OCA].  


==Reference==
==Reference==
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[[Category: wheat]]
[[Category: wheat]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:58:45 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:54 2008''