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TitleCryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 3, Page 288-296, Year 2020
Publish dateMar 2, 2020
AuthorsTomohito Yamada / Toru Yoshida / Akihiro Kawamoto / Kaoru Mitsuoka / Kenji Iwasaki / Hideaki Tsuge /
PubMed AbstractThe iota toxin produced by Clostridium perfringens type E is a binary toxin comprising two independent polypeptides: Ia, an ADP-ribosyltransferase, and Ib, which is involved in cell binding and ...The iota toxin produced by Clostridium perfringens type E is a binary toxin comprising two independent polypeptides: Ia, an ADP-ribosyltransferase, and Ib, which is involved in cell binding and translocation of Ia across the cell membrane. Here we report cryo-EM structures of the translocation channel Ib-pore and its complex with Ia. The high-resolution Ib-pore structure demonstrates a similar structural framework to that of the catalytic ϕ-clamp of the anthrax protective antigen pore. However, the Ia-bound Ib-pore structure shows a unique binding mode of Ia: one Ia binds to the Ib-pore, and the Ia amino-terminal domain forms multiple weak interactions with two additional Ib-pore constriction sites. Furthermore, Ib-binding induces tilting and partial unfolding of the Ia N-terminal α-helix, permitting its extension to the ϕ-clamp gate. This new mechanism of N-terminal unfolding is crucial for protein translocation.
External linksNat Struct Mol Biol / PubMed:32123390
MethodsEM (single particle)
Resolution2.8 - 2.9 Å
Structure data

0713

6klo

EMDB-0713, PDB-6klo:
Complex structure of Iota toxin enzymatic component (Ia) and binding component (Ib) pore with short stem
Method: EM (single particle) / Resolution: 2.8 Å

0720

6klw

EMDB-0720, PDB-6klw:
Complex structure of Iota toxin enzymatic component (Ia) and binding component (Ib) pore with long stem
Method: EM (single particle) / Resolution: 2.9 Å

0721

6klx

EMDB-0721, PDB-6klx:
Pore structure of Iota toxin binding component (Ib)
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • clostridium perfringens (bacteria)
KeywordsTOXIN / Bacterial binary toxin / Protein translocation channel / ADP-ribosylation

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