Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.1/6144
Título: Structure of beta-cinnamomin, a protein toxic to some plant species
Autor: Rodrigues, M.
Archer, Margarida
Martel, P.
Jacquet, Alain
Cravador, A.
Carrondo, Maria A.
Data: 2002
Editora: Blackwell Munksgaard
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 beta-cinnamomin (beta-CIN) from Phytophthora cinnamomi has been determined at 1.8 Angstrom resolution using the molecular-replacement method. beta-CIN has the same overall structure as beta-cryptogein (beta-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 beta-CRY dimer, although with fewer interactions.
Peer review: yes
URI: http://hdl.handle.net/10400.1/6144
DOI: https://dx.doi.org/10.1107/S0907444902010107
ISSN: 0907-4449
Aparece nas colecções:FCT2-Artigos (em revistas ou actas indexadas)

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