1LJP
Crystal Structure of beta-Cinnamomin Elicitin
Summary for 1LJP
Entry DOI | 10.2210/pdb1ljp/pdb |
Descriptor | Beta-elicitin cinnamomin (2 entities in total) |
Functional Keywords | elicitin, sterol carrier protein, phytopathogen, toxin |
Biological source | Phytophthora cinnamomi |
Cellular location | Secreted: P15569 |
Total number of polymer chains | 2 |
Total formula weight | 20599.52 |
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 citation | Rodrigues, 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: 12136143DOI: 10.1107/S0907444902010107 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report