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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
Version:
Publisher's version

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Publisher copy:
10.1038/ncomms11598

Authors


Podobnik, M More by this author
Kisovec, M More by this author
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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
Pages:
Article: 11598
Publication date:
2016-05-12
DOI:
ISSN:
2041-1723
Pubs id:
pubs:623163
Local pid:
info:fedora/pubs:623163
Language:
English
Keywords:

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