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Provedor de dados:  Inra
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
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