Abstract：
: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.
journal_name
Nat Struct Mol Bioljournal_title
Nature structural & molecular biologyauthors
Yamada T,Yoshida T,Kawamoto A,Mitsuoka K,Iwasaki K,Tsuge Hdoi
10.1038/s41594-020-0388-6subject
Has Abstractpub_date
2020-03-01 00:00:00pages
288-296issue
3eissn
1545-9993issn
1545-9985pii
10.1038/s41594-020-0388-6journal_volume
27pub_type
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journal_title：Nature structural & molecular biology
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pub_type： 已发布勘误
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pub_type： 杂志文章,评审
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更新日期：2013-01-01 00:00:00
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pub_type： 杂志文章
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更新日期：2013-05-01 00:00:00
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pub_type： 杂志文章
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更新日期：2013-08-01 00:00:00
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更新日期：2013-02-01 00:00:00
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