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Cryo-EM structures of Ib-pore and Ia-bound Ib-pore


ABSTRACT:

SUBMITTER: Hideaki Tsuge 

PROVIDER: EMPIAR-11265 | biostudies-other |

REPOSITORIES: biostudies-other

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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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