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TitleAtomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.
Journal, issue, pagesStructure, Vol. 28, Issue 8, Page 879-887.e3, Year 2020
Publish dateAug 4, 2020
AuthorsKang Zhou / Shiheng Liu / Nathan J Hardenbrook / Yanxiang Cui / Bryan A Krantz / Z Hong Zhou /
PubMed AbstractPathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA) or octamer (PA) ...Pathogenesis of anthrax disease involves two cytotoxic enzymes-edema factor (EF) and lethal factor (LF)-which are individually recruited by the protective antigen heptamer (PA) or octamer (PA) prechannel and subsequently translocated across channels formed on the endosomal membrane upon exposure to low pH. Here, we report the atomic structures of PA 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.
External linksStructure / PubMed:32521227 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.8 Å
Structure data

EMDB-21365, PDB-6vra:
Anthrax octamer prechannel bound to full-length edema factor
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-21694, PDB-6wjj:
Anthrax octamer prechannel bound to full-length lethal factor
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-ZN:
Unknown entry

Source
  • bacillus anthracis (anthrax bacterium)
KeywordsTRANSLOCASE / anthrax toxin / protective antigen / edema factor / octamer / lethal factor

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