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Structural analysis of cassiicolin, a host-selective protein toxin from Corynespora cassiicola Inra
Barthe, P.; Pujade-Renaud, V.; Breton, F.; Gargani, D.; Thai, R.; Roumestand, C.; De Lamotte, F..
Cassiicolin is a host-selective toxin (HST) produced by the fungus Corynespora cassiicola (strain CCP). It is responsible for the Corynespora leaf fall (CLF) disease, which is among the main pathologies affecting rubber tree (Hevea brasiliensis). Working on purified cassiicolin and using electron microscopy, we have demonstrated that this 27-residue O-glycosylated protein is able to induce cellular damages identical to those induced by the fungus on rubber tree leaves and displays the same host selectivity. The solution structure and disulfide pairing of cassiicolin have been determined using NMR spectroscopy and simulated annealing calculations. Cassiicolin appears to have an original structure with a prolate ellipsoid shape. It adopts an over-all fold...
Tipo: Journal Article Palavras-chave: STRUCTURE 3D HST; NMR STRUCTURE; POST-TRANSLATIONAL MODIFICATIONS; PATHOGENICITY; HOST SELECTIVE TOXIN.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008998eec19&uri=/notices/prodinra1/2008/08/
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Structure of a liganded type 2 wheat non-specific lipid transfer protein and the molecular basis of lipid binding Inra
Hoh, F.; Pons, J.-L.; Gautier, M.F.; De Lamotte, F.; Dumas, C..
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...
Tipo: Journal Article Palavras-chave: PROTEINE DE TRANSFERT DES LIPIDES; LPT; STRUCTURE TRIDIMENSIONNELLE; CUTICULE NS-LTP2; LIPID-TRANSFER PROTEIN; LIPID BINDING.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200711dfadf3&uri=/notices/prodinra1/2009/03/
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