1BWO

THE CRYSTAL STRUCTURE OF WHEAT NON-SPECIFIC TRANSFER PROTEIN COMPLEXED WITH TWO MOLECULES OF PHOSPHOLIPID AT 2.1 A RESOLUTION

Summary for 1BWO

• Entry DOI: 10.2210/pdb1bwo/pdb
• Descriptor: NONSPECIFIC LIPID-TRANSFER PROTEIN, [1-MYRISTOYL-GLYCEROL-3-YL]PHOSPHONYLCHOLINE (3 entities in total)
• Functional Keywords: lipid transfer protein, wheat, lipid binding
• Biological source: Triticum aestivum (bread wheat)
• Total number of polymer chains: 2
• Total formula weight: 21112.06

Authors

Charvolin, D.,Cohen-Addad, C.,Pebay-Peyroula, E. (deposition date: 1998-09-25, release date: 1999-08-27, Last modification date: 2024-11-20)

Primary citation

Charvolin, D.,Douliez, J.P.,Marion, D.,Cohen-Addad, C.,Pebay-Peyroula, E.
The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 A resolution.
Eur.J.Biochem., 264:562-568, 1999

PubMed Abstract: 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.

PubMed: 10491104
DOI: 10.1046/j.1432-1327.1999.00667.x

Experimental method

X-RAY DIFFRACTION (2.1 Å)