1uva | pdb_00001uva

Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa

spinqualitylabelsall models 1uva, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uva is a 1 chain structure with sequence from Oryza sativa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MYR Related: 1bv2, 1rzl, 1mzm, 1uvb, 1uvc Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Lipid binding in rice nonspecific lipid transfer protein-1 complexes from Oryza sativa.,Cheng HC, Cheng PT, Peng P, Lyu PC, Sun YJ Protein Sci. 2004 Sep;13(9):2304-15. Epub 2004 Aug 4. PMID:15295114 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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