Exploring ORFan Domains in Giant Viruses Structure of Mimivirus Sulfhydryl Oxidase R596 英文参考文献.docVIP

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Exploring ORFan Domains in Giant Viruses Structure of Mimivirus Sulfhydryl Oxidase R596 英文参考文献.doc

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Exploring ORFan Domains in Giant Viruses Structure of Mimivirus Sulfhydryl Oxidase R596 英文参考文献

ExploringORFanDomainsinGiantViruses:Structureof MimivirusSulfhydrylOxidaseR596 MottiHakim,DariaEzerina,AssafAlon,OhadVonshak,DeborahFass* DepartmentofStructuralBiology,WeizmannInstituteofScience,Rehovot,Israel Abstract ThemimivirusgenomecontainsmanygenesthatlackhomologsinthesequencedatabaseandarethusknownasORFans. Inaddition,mimivirusgenesthatencodeproteinsbelongingtoknownfoldfamiliesareinsomecasesfusedtodomain- sizedsegmentsthatcannotbeclassified.OnesuchORFanregionispresentinthemimivirusenzymeR596,amemberofthe Erv family of sulfhydryl oxidases. We determined the structure of a variant of full-length R596 and observed that the carboxy-terminal region of R596 assumes a folded, compact domain, demonstrating that these ORFan segments can be stablestructuralunits.Moreover,theR596ORFandomainfoldisnovel,hintingatthepotentialwealthofproteinstructural innovationyettobediscoveredinlargedouble-strandedDNAviruses.InthecontextoftheR596dimer,theORFandomain contributestoformationofabroadcleftenrichedwithexposedaromaticgroupsandbasicsidechains,whichmayfunction inbindingtargetproteinsorlocalizationoftheenzymewithinthevirusfactoryorvirions.Finally,wefindevidenceforan intermoleculardithiol/disulfiderelaywithinthemimivirusR596dimer,thefirstsuchextended,intersubunitredox-activesite identifiedinaviralsulfhydryloxidase. Citation:HakimM,EzerinaD,AlonA,VonshakO,FassD(2012)ExploringORFanDomainsinGiantViruses:StructureofMimivirusSulfhydrylOxidaseR596.PLoS ONE7(11):e50649.doi:10.1371/journal.pone.0050649 Editor:Young-HwaSong,ResearchCenterBorstel,Germany ReceivedJuly3,2012;AcceptedOctober22,2012;PublishedNovember28,2012 Copyright: ? 2012 Hakim etal. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding: This work was supported by the Kimmelman Center for Macromolecular Assemblies. The funder had no role in study design,