1pre
From Proteopedia
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| - | [[Image:1pre.gif|left|200px]] | + | [[Image:1pre.gif|left|200px]] |
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| - | '''PROAEROLYSIN''' | + | {{Structure |
| + | |PDB= 1pre |SIZE=350|CAPTION= <scene name='initialview01'>1pre</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PROAEROLYSIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PRE is a [ | + | 1PRE is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7510043 7510043] |
[[Category: Aeromonas hydrophila]] | [[Category: Aeromonas hydrophila]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: toxin (hemolytic polypeptide)]] | [[Category: toxin (hemolytic polypeptide)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:03 2008'' |
Revision as of 11:28, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROAEROLYSIN
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.
About this Structure
1PRE is a Single protein structure of sequence from Aeromonas hydrophila. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 13:28:03 2008
