Aerolysin

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[[Image:1pre.png|left|200px|thumb|Crystal Structure of Proaerolysin [[1pre]]]]
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<StructureSection load='1pre' size='340' side='right' caption='Proaerolysin dimer (PDB code [[1pre]]).' scene='43/430021/Cv/2'>
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{{STRUCTURE_1pre| PDB=1pre | SIZE=400| SCENE=Aerolysin/Cv/1 |right|CAPTION=Proaerolysin dimer [[1pre]] }}
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[[Aerolysin]] (Aer) is a channel-forming toxin from ''Aeromonas hydrophyla''. It uses GPI-anchored proteins on the cell surface as receptors. Following binding it forms heptamers which insert into the cell membrane producing channels thus causing cell death. It is secreted as an inactive precursor '''proaerolysin''' (proAer) which gets cleaved at Arg-432 by furin to produce the active Aer.<ref>PMID:7510043</ref> For toxins in Proteopedia see [[Toxins]].
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[[Aerolysin]] (Aer) is a channel-forming toxin from ''Aeromonas hydrophyla''. It uses GPI-anchored proteins on the cell surface as receptors. Following binding it forms heptamers which insert into the cell membrane producing channels thus causing cell death. It is secreted as an inactive precursor proaerolysin (proAer) which gets cleaved by furin to produce the active Aer. The images at the left and at the right correspond to one representative Aerolysin, ''i.e.'' the crystal structure of Proaerolysin ([[1pre]]). For toxins in Proteopedia see [[Toxins]].
 
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== 3D Structures of Aerolysin ==
== 3D Structures of Aerolysin ==
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[[Aerolysin 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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=== Aerolysin ===
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[[3g4n]], [[3g4o]] – Aer (mutant)
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=== Proaerolysin ===
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[[1pre]] - proAer<br />
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[[3c0m]], [[3c0n]], [[1z52]] - proAer (mutant)<br />
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[[3c0o]] - proAer (mutant)+mannose-6-phosphate
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Proaerolysin dimer (PDB code 1pre).

Drag the structure with the mouse to rotate

References

  1. Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043 doi:http://dx.doi.org/10.1038/367292a0

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky

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