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Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa

Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan 300, Republic of China

(RECEIVED April 8, 2004; FINAL REVISION May 31, 2004; ACCEPTED June 1, 2004)

Nonspecific lipid transfer proteins (nsLTPs) facilitate the transfer of phospholipids, glycolipids, fatty acids and steroids between membranes, with wide-ranging binding affinities. Three crystal structures of rice nsLTP1 from Oryza sativa, complexed with myristic (MYR), palmitic (PAL) or stearic acid (STE) were determined. The overall structures of the rice nsLTP1 complexes belong to the four-helix bundle folding with a long C-terminal loop. The nsLTP1–MYR and the nsLTP1–STE complexes bind a single fatty acid while the nsLTP1–PAL complex binds two molecules of fatty acids. The C-terminal loop region is elastic in order to accommodate a diverse range of lipid molecules. The lipid molecules interact with the nsLTP1-binding cavity mainly with hydrophobic interactions. Significant conformational changes were observed in the binding cavity and the C-terminal loop of the rice nsLTP1 upon lipid binding.

Keywords: rice nonspecific lipid transfer protein; fatty acid binding; antifungal activity; hydrophobic cavity

Abbreviations: DMPG, dimyristoyl-phosphatidylglycerol • LMPC, lysomyristoyl-phosphatidylcholine • LTP, lipid transfer protein • MYR, myristic acid • NMR, nuclear magnetic resonance • NsLTP, nonspecific lipid transfer protein • PAL, palmitic acid • PCoA, palmitoyl coenzyme A • r.m.s., root-mean-square • STE, stearic acid

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04799704.

Reprint requests to: Yuh-Ju Sun, Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan 300, Republic of China; e-mail: yjsun{at}life.nthu.edu.tw; fax: 886-3-571-5934.

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