1UVB
Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa
Summary for 1UVB
| Entry DOI | 10.2210/pdb1uvb/pdb |
| Related | 1BV2 1MZM 1RZL 1UVA 1UVC |
| Descriptor | NONSPECIFIC LIPID TRANSFER PROTEIN, PALMITOLEIC ACID (3 entities in total) |
| Functional Keywords | lipid transport, ltp 1, pap 1, rice, fatty acid binding |
| Biological source | ORYZA SATIVA (RICE) |
| Total number of polymer chains | 1 |
| Total formula weight | 9428.00 |
| Authors | Cheng, H.-C.,Cheng, P.-T.,Peng, P.,Lyu, P.-C.,Sun, Y.-J. (deposition date: 2004-01-19, release date: 2004-10-19, Last modification date: 2023-12-13) |
| Primary citation | Cheng, H.-C.,Cheng, P.-T.,Peng, P.,Lyu, P.-C.,Sun, Y.-J. Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza Sativa Protein Sci., 13:2304-, 2004 Cited by PubMed 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. PubMed: 15295114DOI: 10.1110/PS.04799704 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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