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1、StructureandfunctionofcytochromesP450:acomparativeanalysisofthreecrystalstructuresCharlesAHasemann',RaviGKurumbail',SekharSBoddupalli2,JulianAPeterson2andJohannDeisenhofer1,2*2DepartmentofBiochemistry,UniversityofTexasSouthwesternMedicalCenter,1HowardHughesMedica
2、lInstituteand5323HarryHinesBoulevard,Dallas,TX75235-9050,USABackground:CytochromesP450catalyzetheoxidationdistributioninthethreestructuresissimilarlyasymmetricofavarietyofhydrophobicsubstrates.Sequenceidentitiesanddefinesamoleculardipole.betweenP450familiesaregen
3、erallylow(10-30%),andconsequently,thestructure-functioncorrelationsamongConclusions:BasedonthiscomparisonwebelievethatP450sarenotclear.ThecrystalstructuresofP450,,rpandallP450swillbefoundtopossessthesametertiarystruc-450thehemoproteindomainofPBM-3wererecentlyture
4、.TheabilitytopreciselypredictotherP450substrate-determined,andarecomparedherewiththepreviouslycontactresiduesislimitedbytheextremestructuralavailablestructureofP450cam.heterogeneityinthesubstrate-recognitionregions.TheResults:Thetopologyofallthreeenzymesisquitesi
5、mi-4450centralI-helixstructuresofP50te,,pandPBM-3sug-lar.Theheme-bindingcorestructureiswellconserved,gestaroleforhelix-associatedsolventmoleculesasaexceptforlocaldifferencesintheIhelices.Thegreatestsourceofcatalyticprotons,distinctfromthemechanismvariationisobser
6、vedinthesubstrate-bindingregions.TheforP450ca,,,,,.WesuggestthattheP450moleculardipolestructuralsuperpositionoftheproteinspermitsanim-mightaidinbothredox-partnerdockingandprotonprovedsequencealignmentofotherP450s.Thechargerecruitmentforcatalysis.Structure15Januar
7、y1995,2:41-62Keywords:crystalstructure,cytochromeP450,electrostatics,hemoprotein,monooxygenaseIntroductionhydroxylationofthebicyclicmonoterpenecamphorCytochromesP450catalyzethemonooxygenationofa(Cl(H160).Thebiochemistryofthisenzymehasbeenvarietyofhydrophobicsubst
8、rates[1,2].P450shavebeenextensivelycharacterized,andthoseresultscorrelatedidentifiedinbacteria,yeast,fungi,worms,plants,insects,withthehigh-resolutionstructure
