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

ABSTRACT: 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.

SUBMITTER: Cheng HC

PROVIDER: S-EPMC2280015 | biostudies-literature | 2004 Sep

REPOSITORIES: biostudies-literature

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

Cheng Hui-Chun HC Cheng Pei-Tsung PT Peng Peiyu P Lyu Ping-Chiang PC Sun Yuh-Ju YJ

Protein science : a publication of the Protein Society 20040804 9

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 si ...[more]

PMID: 15295114

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