1ljp
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(New page: 200px<br /><applet load="1ljp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ljp, resolution 1.80Å" /> '''Crystal Structure of...)
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Revision as of 18:29, 20 November 2007
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Crystal Structure of beta-Cinnamomin Elicitin
Overview
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.
About this Structure
1LJP is a Single protein structure of sequence from Phytophthora cinnamomi. Full crystallographic information is available from OCA.
Reference
Structure of beta-cinnamomin, a protein toxic to some plant species., Rodrigues ML, Archer M, Martel P, Jacquet A, Cravador A, Carrondo MA, Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1314-21. Epub 2002, Jul 20. PMID:12136143
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