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TitleHigh-resolution structure of native toxin A from Clostridioides difficile.
Journal, issue, pagesEMBO Rep, Vol. 23, Issue 1, Page e53597, Year 2022
Publish dateJan 5, 2022
AuthorsAria Aminzadeh / Christian Engelbrecht Larsen / Thomas Boesen / René Jørgensen /
PubMed AbstractClostridioides difficile infections have emerged as the leading cause of healthcare-associated infectious diarrhea. Disease symptoms are mainly caused by the virulence factors, TcdA and TcdB, which ...Clostridioides difficile infections have emerged as the leading cause of healthcare-associated infectious diarrhea. Disease symptoms are mainly caused by the virulence factors, TcdA and TcdB, which are large homologous multidomain proteins. Here, we report a 2.8 Å resolution cryo-EM structure of native TcdA, unveiling its conformation at neutral pH. The structure uncovers the dynamic movement of the CROPs domain which is induced in response to environmental acidification. Furthermore, the structure reveals detailed information about the interaction area between the CROPs domain and the tip of the delivery and receptor-binding domain, which likely serves to shield the C-terminal part of the hydrophobic pore-forming region from solvent exposure. Similarly, extensive interactions between the globular subdomain and the N-terminal part of the pore-forming region suggest that the globular subdomain shields the upper part of the pore-forming region from exposure to the surrounding solvent. Hence, the TcdA structure provides insights into the mechanism of preventing premature unfolding of the pore-forming region at neutral pH, as well as the pH-induced inter-domain dynamics.
External linksEMBO Rep / PubMed:34817920 / PubMed Central
MethodsEM (single particle)
Resolution2.83 Å
Structure data

13574

7pog

EMDB-13574, PDB-7pog:
High-resolution structure of native toxin A from Clostridioides difficile
Method: EM (single particle) / Resolution: 2.83 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • clostridioides difficile (bacteria)
  • Peptoclostridium difficile (bacteria)
KeywordsTOXIN / glucosyltransferase

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