Lipid-transfer proteins from plants: structure and binding properties.
Plant cells contain lipid-transfer proteins (LTPs) able to transfer phospholipids between membranes in vitro. Plant LTPs share in common structural and functional features. Recent structural studies carried out by NMR and X-ray crystallography on an LTP isolated from maize seeds have showed that this protein involves four helices packed against a C-terminal region and stabilized by four disulfide bridges. A most striking feature of this structure is the existence of an internal hydrophobic cavity running through the whole molecule and able to accommodate acyl chains. It was thus of interest to study the ability of maize LTP to bind hydrophobic ligands such as acyl chains or lysophosphatidylcholine and to determine the effect of this binding on phospholipid transfer. The binding abilities of maize LTP, presented in this paper, are discussed and compared to those of lipid-binding proteins from animal tissues.
Guerbette
F
F
Laboratoire de Physiologie Cellulaire et Moléculaire, Unit CNRS 2135, Université Pierre et Marie Curie, Paris, France.
Grosbois
M
M
Jolliot-Croquin
A
A
Kader
J C
JC
Zachowski
A
A
D000214:Acyl Coenzyme A / Q000737:chemistry; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000737:chemistry*; D004305:Dose-Response Relationship, Drug; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D003313:Zea mays / Q000737:chemistry
D000214:Acyl Coenzyme A; D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant