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Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly

Abstract:

The invertebrate cytolysin lysenin is a member of the aerolysin family of pore-forming toxins that includes many representatives from pathogenic bacteria. Here we report the crystal structure of the lysenin pore and provide insights into its assembly mechanism. The lysenin pore is assembled from nine monomers via dramatic reorganization of almost half of the monomeric subunit structure leading to a β-barrel pore ~10 nm long and 1.6–2.5 nm wide. The lysenin pore is devoid of additional luminal...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/ncomms11598

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Grant:
ERC IMPRESS (26,851)
FP7/2007–2013) under BioStruct-X (grant agreement N283570
Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Communications Journal website
Volume:
7
Article number:
11598
Publication date:
2016-05-12
Acceptance date:
2016-04-11
DOI:
ISSN:
2041-1723
Source identifiers:
623163
Language:
English
Keywords:
Pubs id:
pubs:623163
UUID:
uuid:51fe7e4f-1b09-4438-b1a9-f17643687b9d
Local pid:
info:fedora/pubs:623163
Deposit date:
2016-09-01

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