1pre: Difference between revisions
New page: left|200px<br /><applet load="1pre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pre, resolution 2.8Å" /> '''PROAEROLYSIN'''<br />... |
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[[Image:1pre.gif|left|200px]]<br /><applet load="1pre" size=" | [[Image:1pre.gif|left|200px]]<br /><applet load="1pre" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pre, resolution 2.8Å" /> | caption="1pre, resolution 2.8Å" /> | ||
'''PROAEROLYSIN'''<br /> | '''PROAEROLYSIN'''<br /> | ||
==Overview== | ==Overview== | ||
Aerolysin is chiefly responsible for the pathogenicity of Aeromonas | Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels. | ||
==About this Structure== | ==About this Structure== | ||
1PRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http:// | 1PRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila Aeromonas hydrophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Aeromonas hydrophila]] | [[Category: Aeromonas hydrophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Buckley, J | [[Category: Buckley, J T.]] | ||
[[Category: Parker, M | [[Category: Parker, M W.]] | ||
[[Category: Postma, J | [[Category: Postma, J P.M.]] | ||
[[Category: Tsernoglou, D.]] | [[Category: Tsernoglou, D.]] | ||
[[Category: Tucker, A | [[Category: Tucker, A D.]] | ||
[[Category: signal]] | [[Category: signal]] | ||
[[Category: toxin (hemolytic polypeptide)]] | [[Category: toxin (hemolytic polypeptide)]] | ||
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Revision as of 15:31, 21 February 2008
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PROAEROLYSIN
OverviewOverview
Aerolysin is chiefly responsible for the pathogenicity of Aeromonas hydrophila, a bacterium associated with diarrhoeal diseases and deep wound infections. Like many other microbial toxins, the protein changes in a multistep process from a completely water-soluble form to produce a transmembrane channel that destroys sensitive cells by breaking their permeability barriers. Here we describe the structure of proaerolysin determined by X-ray crystallography at 2.8 A resolution. The protoxin (M(r) 52,000) adopts a novel protein fold. Images of an aerolysin oligomer derived from electron microscopy have assisted in constructing a model of the membrane channel and have led to the proposal of a scheme to account for insertion of the protein into lipid bilayers to form ion channels.
About this StructureAbout this Structure
1PRE is a Single protein structure of sequence from Aeromonas hydrophila. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states., Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D, Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043
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