1bwo: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwo OCA], [http://www.ebi.ac.uk/pdbsum/1bwo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bwo RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Cohen-Addad, C.]] | [[Category: Cohen-Addad, C.]] | ||
[[Category: Pebay-Peyroula, E.]] | [[Category: Pebay-Peyroula, E.]] | ||
[[Category: crystallography]] | [[Category: crystallography]] | ||
[[Category: lipid binding]] | [[Category: lipid binding]] | ||
| Line 31: | Line 33: | ||
[[Category: wheat]] | [[Category: wheat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:46 2008'' | ||
Revision as of 16:09, 30 March 2008
| |||||||||||||
| 1bwo, resolution 2.10Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | LPC | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Sun Mar 30 19:09:46 2008
