1TUK
Crystal structure of liganded type 2 non specific lipid transfer protein from wheat
Summary for 1TUK
| Entry DOI | 10.2210/pdb1tuk/pdb |
| Related | 1N89 |
| Descriptor | Nonspecific lipid-transfer protein 2G, IODIDE ION, 1-MYRISTOYL-2-HYDROXY-SN-GLYCERO-3-[PHOSPHO-RAC-(1-GLYCEROL)], ... (4 entities in total) |
| Functional Keywords | ns-ltp2, lipid transfer protein, lipid transport |
| Biological source | Triticum aestivum (bread wheat) |
| Cellular location | Secreted, cell wall : P82900 |
| Total number of polymer chains | 1 |
| Total formula weight | 8206.86 |
| Authors | Hoh, F.,Pons, J.L.,Gautier, M.F.,De Lamotte, F.,Dumas, C. (deposition date: 2004-06-25, release date: 2005-04-05, Last modification date: 2024-10-30) |
| Primary citation | Hoh, F.,Pons, J.L.,Gautier, M.F.,de Lamotte, F.,Dumas, C. Structure of a liganded type 2 non-specific lipid-transfer protein from wheat and the molecular basis of lipid binding. Acta Crystallogr.,Sect.D, 61:397-406, 2005 Cited by PubMed Abstract: In plants, a family of ubiquitous proteins named non-specific lipid-transfer proteins (ns-LTPs) facilitates the transfer of fatty acids, phospholipids and steroids between membranes. Recent data suggest that these secreted proteins play a key role in the formation of cuticular wax layers and in defence mechanisms against pathogens. In this study, X-ray crystallography has been used to examine the structural details of the interaction between a wheat type 2 ns-LTP and a lipid, L-alpha-palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 A resolution by direct methods. The typical alpha-helical bundle fold of this protein is maintained by four disulfide bridges and delineates two hydrophobic cavities. The inner surface of the main cavity is lined by non-polar residues that provide a hydrophobic environment for the palmitoyl moiety of the lipid. The head-group region of this lipid protrudes from the surface and makes several polar interactions with a conserved patch of basic residues at the entrance of the pocket. The alkyl chain of a second lipid is bound within an adjacent smaller cavity. The structure shows that binding of the lipid tails to the protein involves extensive hydrophobic interactions. PubMed: 15805594DOI: 10.1107/S0907444905000417 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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