Summary: Aerolysin toxin
This is the Wikipedia entry entitled "Aerolysin". More...
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Aerolysin Edit Wikipedia article
In molecular biology, aerolysin is a cytolytic pore-forming toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections. The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction of the membrane permeability barrier and osmotic lysis. The structure of proaerolysin has been determined to 2.8A resolution and shows the protoxin to adopt a novel fold. Images of an aerolysin oligomer derived from electron microscopy and molecular dynamics simulations have helped to construct a model of the protein in its heptameric conformation, and to outline a mechanism by which this assembly might insert into lipid bilayers to form ion channels.
- Howard SP, Garland WJ, Green MJ, Buckley JT (June 1987). "Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila". J. Bacteriol. 169 (6): 2869–71. PMC 212202. PMID 3584074.
- Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D (January 1994). "Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states". Nature 367 (6460): 292–5. doi:10.1038/367292a0. PMID 7510043.
- Degiacomi MT, Iacovache I,Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M (August 2013). "Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism". Nature Chemical Biology 9 (6460): 623–629. doi:10.1038/nchembio.1312. PMID 23912165.
Aerolysin toxin Provide feedback
This family represents the pore forming lobe of aerolysin.
Internal database links
|Similarity to PfamA using HHSearch:||ETX_MTX2|
External database links
|Transporter classification:||1.C.14 1.C.3 1.C.4|
This tab holds annotation information from the InterPro database.
InterPro entry IPR005830
This family represents the pore forming lobe of aerolysin, and the related toxins haemolysin and the leukocidin S subunit.
Aerolysin [PUBMED:3584074] is a cytolytic toxin exported by Aeromonas hydrophila, a Gram-negative bacterium associated with diarrhoeal diseases and deep wound infections [PUBMED:7510043]. The mature toxin binds to eukaryotic cells and aggregates to form holes (approximately 3 nm in diameter) leading to the destruction of the membrane permeability barrier and osmotic lysis. The structure of proaerolysin has been determined to 2.8A resolution and shows the protoxin to adopt a novel fold [PUBMED:7510043]. Images of an aerolysin oligomer derived from electron microscopy have helped to construct a model of the protein and to outline a mechanism by which it might insert into lipid bilayers to form ion channels [PUBMED:7510043].
|Cellular component||extracellular region (GO:0005576)|
|Biological process||pathogenesis (GO:0009405)|
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EGFdomains, and finally a single
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Curation and family details
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||14|
|Number in full:||252|
|Average length of the domain:||219.70 aa|
|Average identity of full alignment:||45 %|
|Average coverage of the sequence by the domain:||72.35 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Aerolysin domain has been found. There are 14 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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