1bwo
From Proteopedia
(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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| - | [[Image:1bwo.jpg|left|200px]]<br /><applet load="1bwo" size=" | + | [[Image:1bwo.jpg|left|200px]]<br /><applet load="1bwo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bwo, resolution 2.10Å" /> | caption="1bwo, resolution 2.10Å" /> | ||
'''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 | + | 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:// | + | 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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:54 2008'' |
Revision as of 09:59, 21 February 2008
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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 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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