0000000000134028

AUTHOR

Thierry Prangé

0000-0002-7129-7396

showing 4 related works from this author

Purification, crystallization and preliminary X-ray studies of sylvaticin, an elicitin-like protein from Pythium sylvaticum.

2003

Sylvaticin belongs to the elicitin family. These 10 kDa oomycetous proteins induce a hypersensitive response in plants, including necrosis and cell death, but subsequently leading to a non-specific systemic acquired resistance (SAR) against other pathogens. Sylvaticin has been crystallized using PEG 2000 MME as a precipitant agent in the presence of nickel chloride. The crystals belong to space group C2, with unit-cell parameters a = 99.29, b = 25.67, c = 67.45 A, beta = 99.66 degrees. Diffraction data were recorded to 2.1 A resolution at a synchrotron-radiation source.

Hypersensitive responseStereochemistryProtein ConformationPythiumBiologyCrystallography X-Raylaw.inventionPolyethylene GlycolsProtein structureStructural BiologylawNickelPEG ratioCrystallizationFuransAlgal ProteinsX-rayProteinsElicitinGeneral Medicinebiology.organism_classificationCrystallographySolventsPythium sylvaticumSystemic acquired resistanceSynchrotronsActa crystallographica. Section D, Biological crystallography
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The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site.

2002

Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle.

Models MolecularStereochemistryMolecular Sequence DataBiologyFungal Proteinschemistry.chemical_compoundStructural BiologyAmino Acid SequenceOomyceteBinding SitesMolecular StructureSequence Homology Amino AcidCholesterolPhytophthora cryptogeaResolution (electron density)Algal ProteinsActive siteGeneral Medicinebiology.organism_classificationSterolElicitorSterolsSterol carrier proteinCholesterolBiochemistrychemistrybiology.proteinCarrier ProteinsActa crystallographica. Section D, Biological crystallography
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Fatty acids bind to the fungal elicitor cryptogein and compete with sterols

2001

Abstract Cryptogein is a proteinaceous elicitor of plant defense reactions which also exhibits sterol carrier properties. In this study, we report that this protein binds fatty acids. The stoichiometry of the fatty acid–cryptogein complex is 1:1. Linoleic acid and dehydroergosterol compete for the same site, but elicitin affinity is 27 times lower for fatty acid than for sterol. We show that C7 to C12 saturated and C16 to C22 unsaturated fatty acids are the best ligands. The presence of double bonds markedly increases the affinity of cryptogein for fatty acids. A comparison between elicitins and known lipid transfer proteins is discussed.

Phytophthora0106 biological sciencesDouble bondLinoleic acidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyBinding Competitive01 natural sciencesBiochemistryFungal ProteinsLinoleic AcidLIAISON MOLECULAIREStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolGeneticsPlant defense against herbivoryMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSSterol030304 developmental biologychemistry.chemical_classification0303 health sciencesAlgal ProteinsFatty AcidsProteinsFatty acidLipid–protein interactionElicitinCell BiologyFatty acidElicitinSterol3. Good healthElicitorSterolschemistryBiochemistrylipids (amino acids peptides and proteins)Plant lipid transfer proteinsProtein Binding010606 plant biology & botany
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Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor fromPythium oligandrum

2000

Oligandrin is a 10 kDa acidic protein produced by the fungus micromycete Pythium oligandrum and is a member of the alpha-elicitin group, with sterol- and lipid-carrier properties. Oligandrin has been crystallized at 290 K using PEG 4000 as a precipitant. A cholesterol complex was obtained under the same conditions. The space group of the crystals at low temperature (100 K) is C222, with unit-cell parameters a = 94.0, b = 171.1, c = 55.3 A. Four molecules are present in the asymmetric unit. Data from the free and cholesterol-complexed forms were recorded at synchrotron sources to resolutions of 2.4 (uncomplexed) and 1.9 A (complexed), respectively.

Protein ConformationPythiumElicitinGeneral MedicineBiologyCrystallography X-Raybiology.organism_classificationSterolElicitorlaw.inventionFungal ProteinsSterolsCrystallographyCholesterolSterol carrier proteinStructural BiologylawPEG ratioIntercellular Signaling Peptides and ProteinsMoleculeElectrophoresis Polyacrylamide GelCrystallizationCarrier ProteinsCrystallizationPythium oligandrumActa Crystallographica Section D Biological Crystallography
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