1ljp | pdb_00001ljp

Crystal Structure of beta-Cinnamomin Elicitin

spinqualitylabelsall models 1ljp, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ljp is a 2 chain structure with sequence from Cinnamon fungus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: cin1B (Cinnamon fungus) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ELIB_PHYCI] Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. Elicitins are able to load, carry, and transfer sterols between membranes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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