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dc.contributor.authorZhou, K.
dc.contributor.authorHardenbrook, N.J.
dc.contributor.authorKrantz, B.A.
dc.date.accessioned2020-07-07T19:59:45Z
dc.date.available2020-07-07T19:59:45Z
dc.date.issued2020
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85086940547&doi=10.1016%2fj.str.2020.05.009&partnerID=40&md5=2e660e4d918b128178002b48fae2ca43
dc.identifier.urihttp://hdl.handle.net/10713/13241
dc.description.abstractPathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA7) or octamer (PA8) prechannel and subsequently translocated across channels formed on the endosomal membrane upon exposure to low pH. Here, we report the atomic structures of PA8 prechannel-bound full-length EF and LF. In this pretranslocation state, the N-terminal segment of both factors refolds into an α helix engaged in the α clamp of the prechannel. Recruitment to the PA prechannel exposes an originally buried β strand of both toxins and enables domain organization of EF. Many interactions occur on domain interfaces in both PA prechannel-bound EF and LF, leading to toxin compaction prior to translocation. Our results provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.en_US
dc.description.sponsorshipThis work was supported in part by grants from the National Science Foundation (NSF, under grant no. DMR-1548924 ) and by grants from the National Institutes of Health ( R01GM071940/AI094386/DE025567 to Z.H.Z. and R21AI124020 to B.A.K.) and the Training Program in Integrative Membrane Biology at the University of Maryland , Baltimore ( T32GM008181 ).en_US
dc.description.urihttps://doi.org/10.1016/j.str.2020.05.009en_US
dc.language.isoen_USen_US
dc.publisherCell Pressen_US
dc.relation.ispartofStructure
dc.subjectanthrax prechannelen_US
dc.subjectcomplex structureen_US
dc.subjectcryo-EMen_US
dc.subjectedema factoren_US
dc.subjectlethal factoren_US
dc.titleAtomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factorsen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.str.2020.05.009
dc.identifier.pmid32521227


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