1pre: Difference between revisions

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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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1pre.gif|left|200px]]<br /><applet load="1pre" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1pre, resolution 2.8&Aring;" />
caption="1pre, resolution 2.8&Aring;" />
'''PROAEROLYSIN'''<br />
'''PROAEROLYSIN'''<br />


==Overview==
==Overview==
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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PRE OCA].  
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.T.]]
[[Category: Buckley, J T.]]
[[Category: Parker, M.W.]]
[[Category: Parker, M W.]]
[[Category: Postma, J.P.M.]]
[[Category: Postma, J P.M.]]
[[Category: Tsernoglou, D.]]
[[Category: Tsernoglou, D.]]
[[Category: Tucker, A.D.]]
[[Category: Tucker, A D.]]
[[Category: signal]]
[[Category: signal]]
[[Category: toxin (hemolytic polypeptide)]]
[[Category: toxin (hemolytic polypeptide)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:03:25 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:52 2008''