Cryo-EM structures of Ib-pore and Ia-bound Ib-pore
Ontology highlight
ABSTRACT:
SUBMITTER: Hideaki Tsuge
PROVIDER: EMPIAR-11265 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex.
Yamada Tomohito T Yoshida Toru T Kawamoto Akihiro A Mitsuoka Kaoru K Iwasaki Kenji K Tsuge Hideaki H
Nature structural & molecular biology 20200302 3
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, ...[more]
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