| 词条 | Aerolysin |
| 释义 |
| Symbol = Aerolysin | Name = Aerolysin | image = PDB 1pre EBI.jpg | width = | caption = proaerolysin | Pfam = PF01117 | Pfam_clan = CL0345 | InterPro = IPR005830 | SMART = | PROSITE = PDOC00247 | MEROPS = | SCOP = 1pre | TCDB = 1.C.4 | OPM family = 35 | OPM protein = 5jzt | CAZy = | CDD = }} 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.[1][2] 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.[3] Images of an aerolysin oligomer derived from electron microscopy 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.[4] References1. ^{{cite journal |vauthors=Howard SP, Garland WJ, Green MJ, Buckley JT | title = Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila | journal = J. Bacteriol. | volume = 169 | issue = 6 | pages = 2869–71 |date=June 1987 | pmid = 3584074 | pmc = 212202 | doi = 10.1128/jb.169.6.2869-2871.1987| url = }} {{InterPro content|IPR005830}}2. ^{{cite journal |vauthors=Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D | title = Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states | journal = Nature | volume = 367 | issue = 6460 | pages = 292–5 |date=January 1994 | pmid = 7510043 | doi = 10.1038/367292a0 | url = }} 3. ^{{cite journal |vauthors=Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D | title = Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states | journal = Nature | volume = 367 | issue = 6460 | pages = 292–5 |date=January 1994 | pmid = 7510043 | doi = 10.1038/367292a0 | url = }} 4. ^{{cite journal |vauthors=Degiacomi MT, Iacovache I, Pernot L, Chami M, Kudryashev M, Stahlberg H, van der Goot FG, Dal Peraro M | title = Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. The gene for aerolysin have been shown to undergo Horizontal gene transfer from prokaryotes to eukaryotes. | journal = Nature Chemical Biology | volume = 9| issue = 6460 | pages = 623–629 |date=August 2013| pmid = 23912165| doi = 10.1038/nchembio.1312 | url = http://www.nature.com/nchembio/journal/v9/n10/full/nchembio.1312.html}} 1 : Protein domains |
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