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1LJP

Crystal Structure of beta-Cinnamomin Elicitin

Summary for 1LJP
Entry DOI10.2210/pdb1ljp/pdb
DescriptorBeta-elicitin cinnamomin (2 entities in total)
Functional Keywordselicitin, sterol carrier protein, phytopathogen, toxin
Biological sourcePhytophthora cinnamomi
Cellular locationSecreted: P15569
Total number of polymer chains2
Total formula weight20599.52
Authors
Rodrigues, M.L.,Archer, M.,Martel, P.,Jacquet, A.,Cravador, A.,Carrondo, M.A. (deposition date: 2002-04-22, release date: 2002-07-31, Last modification date: 2024-11-13)
Primary citationRodrigues, M.L.,Archer, M.,Martel, P.,Jacquet, A.,Cravador, A.,Carrondo, M.A.
Structure of beta-cinnamomin, a protein toxic to some plant species.
Acta Crystallogr.,Sect.D, 58:1314-1321, 2002
Cited by
PubMed Abstract: 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 A 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.
PubMed: 12136143
DOI: 10.1107/S0907444902010107
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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