Ab Initio Modeling of the Herpesvirus VP26 Core Domain Assessed by CryoEM Density 英文参考文献.docVIP

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Ab Initio Modeling of the Herpesvirus VP26 Core Domain Assessed by CryoEM Density 英文参考文献.doc

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Ab Initio Modeling of the Herpesvirus VP26 Core Domain Assessed by CryoEM Density 英文参考文献

AbInitioModelingoftheHerpesvirusVP26 CoreDomainAssessedbyCryoEMDensity Matthew L.Baker1,Wen Jiang2,William J.Wedemeyer3,Frazer J.Rixon4,David Baker5,Wah Chiu1* 1NationalCenterforMacromolecularImaging,VernaandMarrsMcLeanDepartmentofBiochemistryandMolecularBiology,BaylorCollegeofMedicine,Houston,Texas, UnitedStatesofAmerica,2DepartmentofBiologicalSciences,PurdueUniversity,WestLafayette,Indiana,UnitedStatesofAmerica,3DepartmentofBiochemistry,Michigan StateUniversity,East Lansing, Michigan, United States ofAmerica, 4MRC Virology Unit, Institute of Virology, Glasgow, United Kingdom, 5Department ofBiochemistry, UniversityofWashington,Seattle,Washington,UnitedStatesofAmerica Effortsinstructuralbiologyhavetargetedthesystematicdeterminationofallproteinstructuresthroughexperimental determination or modeling. In recent years, 3-D electron cryomicroscopy (cryoEM) has assumed an increasingly importantroleindeterminingthestructuresoftheselargemacromolecularassembliestointermediateresolutions(6– 10A).? Whilethesestructuresprovideasnapshotoftheassemblyanditscomponentsinwell-definedfunctionalstates, theresolutionlimitstheabilitytobuildaccuratestructuralmodels.Incontrast,sequence-basedmodelingtechniques are capable of producing relatively robust structural models for isolated proteins or domains. In this work, we developed and applied a hybrid modeling approach, utilizing cryoEM density and ab initio modeling to produce a structuralmodelforthecoredomainofaherpesvirusstructuralprotein,VP26.Specifically,thismethod,firsttestedon simulateddata,utilizesthecryoEMdensitymapasageometricalconstraintinidentifyingthemostnative-likemodels fromagalleryofmodelsgeneratedbyabinitiomodeling.TheresultingmodelforthecoredomainofVP26,basedon the 8.5-A? resolution herpes simplex virus type 1 (HSV-1) capsid cryoEM structure and mutational data, exhibited a novelfold.Additionally,thecoredomainofVP26appearedtohaveacomplementaryinterfacetotheknownupper- domainstructureofVP5,itscognatebindingpartner.Whi