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Data/hora: 08/06/2017 17:11:13 Provedor de dados: 189 País: France Título: Structure of a liganded type 2 wheat non-specific lipid transfer protein and the molecular basis of lipid binding Autores: Hoh, F.; Pons, J.-L.; Gautier, M.F.; De Lamotte, F.; Dumas, C. Data: 2005 Ano: 2005 Palavras-chave: PROTEINE DE TRANSFERT DES LIPIDES; LPT; STRUCTURE TRIDIMENSIONNELLE; CUTICULE NS-LTP2; LIPID-TRANSFER PROTEIN; LIPID BINDING. Resumo: 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-α--palmitoyl-phosphatidyl glycerol. This crystal structure was solved ab initio at 1.12 Å resolution by direct methods. The typical α--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. Tipo: Journal Article Idioma: Inglês Identificador: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200711dfadf3&uri=/notices /prodinra1/2009/03/ Fonte: Acta Crystallographica Section D Biological Crystallography. 2005, 61 (4) : 397-406