1ljp: Difference between revisions

Revision as of 14:45, 21 February 2008

Crystal Structure of beta-Cinnamomin Elicitin

OverviewOverview

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 StructureAbout this Structure

1LJP is a Single protein structure of sequence from Phytophthora cinnamomi. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:45:34 2008

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OCA

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-[[Image:1ljp.jpg|left|200px]]<br /><applet load="1ljp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ljp.jpg|left|200px]]<br /><applet load="1ljp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ljp, resolution 1.80&Aring;" />
 '''Crystal Structure of beta-Cinnamomin Elicitin'''<br />
 ==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.
+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==
-LJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LJP OCA].
+LJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJP OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Archer, M.]]
-[[Category: Carrondo, M.A.]]
+[[Category: Carrondo, M A.]]
 [[Category: Cravador, A.]]
 [[Category: Jacquet, A.]]
 [[Category: Martel, P.]]
-[[Category: Rodrigues, M.L.]]
+[[Category: Rodrigues, M L.]]
 [[Category: elicitin]]
 [[Category: phytopathogen]]
 [[Category: sterol carrier protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:36:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:34 2008''