Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.1/1218
Título: Structure of ß-cinnamomin, a protein toxic to some plant species
Autor: Rodrigues, Maria Luisa
Archer, Margarida
Martel, Paulo
Jacquet, Alain
Cravador, A.
Carrondo, Maria A.
Palavras-chave: Beta-cinnamomin
Elicitins
Data: 2002
Citação: Rodrigues, Maria L.; Archer, Margarida; Martel, Paulo; Jacquet, Alain; Cravador, Alfredo; Carrondo, Maria A. Structure of ß-cinnamomin, a protein toxic to some plant species. Acta Crystallographica. Section D. Biological Crystallography, 58, 8, 1314-1321, 2002.
Resumo: Phytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant -cinnamomin ( -CIN) from Phytophthora cinnamomi has been determined at 1.8 A Ê resolution using the molecularreplacement method. -CIN has the same overall structure as -cryptogein ( -CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from -CRY dimer, although with fewer interactions.
Peer review: yes
URI: http://hdl.handle.net/10400.1/1218
ISSN: 09074449
Aparece nas colecções:FCT2-Artigos (em revistas ou actas indexadas)

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