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The Aerolysin Family [Function: Non-specific diffusion channels] Seed alignment | Full alignment | Pfam page | TC-DB page

Aerolysin is a heptamer where seven monomers form a ß-barrel with 14 strands at the outer membrane of Aeromonas hydrophila. The aerolysin pore is more stable due its concentric ß-barrel fold.


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Literature references


Central residues of the amphipathic ß-hairpin loop control the properties of Clostridium perfringens epsilon-toxin channel
Biochim Biophys Acta Biomembr. 2020 Sep 1;1862(9):183364. doi: 10.1016/j.bbamem.2020.183364. Epub 2020 May 22.
PMID: 32450142

Single-molecule sensing of peptides and nucleic acids by engineered aerolysin nanopores
Nat Commun. 2019 Oct 29;10(1):4918. doi: 10.1038/s41467-019-12690-9.
PMID: 31664022

Insight into the Structural Dynamics of the Lysenin During Prepore-to-Pore Transition Using Hydrogen-Deuterium Exchange Mass Spectrometry
Toxins (Basel). 2019 Aug 7;11(8):462. doi: 10.3390/toxins11080462.
PMID: 31394843

The pore structure of Clostridium perfringens epsilon toxin
Nat Commun. 2019 Jun 14;10(1):2641. doi: 10.1038/s41467-019-10645-8.
PMID: 31201325

Enterotoxic Clostridia: Clostridium perfringens Enteric Diseases
Microbiol Spectr. 2018 Sep;6(5):10.1128/microbiolspec.GPP3-0003-2017. doi: 10.1128/microbiolspec.GPP3-0003-2017.
PMID: 30238869

Rationally Designed Sensing Selectivity and Sensitivity of an Aerolysin Nanopore via Site-Directed Mutagenesis
ACS Sens. 2018 Apr 27;3(4):779-783. doi: 10.1021/acssensors.8b00021. Epub 2018 Apr 17.
PMID: 29619834

Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family
Sci Rep. 2017 Oct 24;7(1):13932. doi: 10.1038/s41598-017-13714-4.
PMID: 29066778

Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process
Nat Commun. 2016 Jul 13;7:12062. doi: 10.1038/ncomms12062.
PMID: 27405240

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Nat Commun. 2016 May 12;7:11598. doi: 10.1038/ncomms11598.
PMID: 27176125

Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein
Nat Commun. 2016 Apr 6;7:11293. doi: 10.1038/ncomms11293.
PMID: 27048994

Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore
ACS Nano. 2015 Sep 22;9(9):9050-61. doi: 10.1021/acsnano.5b03053. Epub 2015 Aug 28.
PMID: 26302243

Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism
Nat Chem Biol. 2013 Oct;9(10):623-9. doi: 10.1038/nchembio.1312. Epub 2013 Aug 4.
PMID: 23912165

Epsilon toxin: a fascinating pore-forming toxin
FEBS J. 2011 Dec;278(23):4602-15. doi: 10.1111/j.1742-4658.2011.08145.x. Epub 2011 May 25.
PMID: 21535407

Pore-forming activity of alpha-toxin is essential for clostridium septicum-mediated myonecrosis
Infect Immun. 2009 Mar;77(3):943-51. doi: 10.1128/IAI.01267-08. Epub 2009 Jan 12.
PMID: 19139192

A rivet model for channel formation by aerolysin-like pore-forming toxins
EMBO J. 2006 Feb 8;25(3):457-66. doi: 10.1038/sj.emboj.7600959. Epub 2006 Jan 19.
PMID: 16424900

Proteins in this family with 3D-structure
View Entry
Description
Organism
Length
# strands
Outer membrane protein A
Aeromonas hydrophila
493
14


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