Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
26 04 2019
26 04 2019
Historique:
received:
17
04
2018
accepted:
05
04
2019
entrez:
28
4
2019
pubmed:
28
4
2019
medline:
14
5
2019
Statut:
epublish
Résumé
ABC toxins are pore-forming virulence factors produced by pathogenic bacteria. YenTcA is the pore-forming and membrane binding A subunit of the ABC toxin YenTc, produced by the insect pathogen Yersinia entomophaga. Here we present cryo-EM structures of YenTcA, purified from the native source. The soluble pre-pore structure, determined at an average resolution of 4.4 Å, reveals a pentameric assembly that in contrast to other characterised ABC toxins is formed by two TcA-like proteins (YenA1 and YenA2) and decorated by two endochitinases (Chi1 and Chi2). We also identify conformational changes that accompany membrane pore formation by visualising YenTcA inserted into liposomes. A clear outward rotation of the Chi1 subunits allows for access of the protruding translocation pore to the membrane. Our results highlight structural and functional diversity within the ABC toxin subfamily, explaining how different ABC toxins are capable of recognising diverse hosts.
Identifiants
pubmed: 31028251
doi: 10.1038/s41467-019-09890-8
pii: 10.1038/s41467-019-09890-8
pmc: PMC6486591
doi:
Substances chimiques
Bacterial Proteins
0
Liposomes
0
Toxins, Biological
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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