In Silico Characterization and Homology Modeling of Thylakoidbound Ascorbate Peroxidase from a Drought Tolerant Wheat Cultivar-中国期刊网

摘要 Ascorbateperoxidase,ahaemprotein(EC1.11.1.11),efficientlyscavengeshydrogenperoxide(H2O2)incytosolandchloroplastsofplants.Inthisstudy,afulllengthcodingsequenceofthylakoid-boundascorbateperoxidasecDNA(TatAPX)wasclonedfromadroughttolerantwheatcultivarC306.HomologymodelingoftheTatAPXproteinwasperformedbyusingthetemplatecrystalstructureofchloroplasticascorbateperoxidasefromtobaccoplant(PDB:1IYN).ThemodelstructurewasfurtherrefinedbymolecularmechanicsanddynamicmethodsusingvarioustoolssuchasPROCHECK,ProSAandVerify3D.ThepredictedmodelwasthentestedfordockingwithH2O2,thesubstrateforTatAPXenzyme.TheresultsrevealedthatArg233andGlu255inthepredictedactivesiteoftheenzymearetwoimportantaminoacidresiduesresponsibleforstronghydrogenbondingaffinitywithH2O2,whichmightplayanimportantroleinscavengingofH2O2fromtheplantsystem.

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In Silico Characterization and Homology Modeling of Thylakoidbound Ascorbate Peroxidase from a Drought Tolerant Wheat Cultivar

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In Silico Characterization and Homology Modeling of Thylakoidbound Ascorbate Peroxidase from a Drought Tolerant Wheat Cultivar

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