3c0o
From Proteopedia
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|PDB= 3c0o |SIZE=350|CAPTION= <scene name='initialview01'>3c0o</scene>, resolution 2.50Å | |PDB= 3c0o |SIZE=350|CAPTION= <scene name='initialview01'>3c0o</scene>, resolution 2.50Å | ||
|SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Residue+A+600'>AC1</scene>, <scene name='pdbsite=AC2:M6p+Binding+Site+For+Residue+A+501'>AC2</scene> and <scene name='pdbsite=AC3:M6p+Binding+Site+For+Residue+B+502'>AC3</scene> | |SITE= <scene name='pdbsite=AC1:Act+Binding+Site+For+Residue+A+600'>AC1</scene>, <scene name='pdbsite=AC2:M6p+Binding+Site+For+Residue+A+501'>AC2</scene> and <scene name='pdbsite=AC3:M6p+Binding+Site+For+Residue+B+502'>AC3</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= aerA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 Aeromonas hydrophila]) | |GENE= aerA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644 Aeromonas hydrophila]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3c0m|3C0M]], [[3c0n|3C0N]], [[1pre|1PRE]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c0o OCA], [http://www.ebi.ac.uk/pdbsum/3c0o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c0o RCSB]</span> | ||
}} | }} | ||
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[[Category: Schiltz, M.]] | [[Category: Schiltz, M.]] | ||
[[Category: Thurnheer, S.]] | [[Category: Thurnheer, S.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: M6P]] | ||
[[Category: cytolytic toxin]] | [[Category: cytolytic toxin]] | ||
[[Category: pore-forming toxin]] | [[Category: pore-forming toxin]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:29:59 2008'' |
Revision as of 02:30, 31 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , | ||||||
| Gene: | aerA (Aeromonas hydrophila) | ||||||
| Related: | 3C0M, 3C0N, 1PRE
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the proaerolysin mutant Y221G complexed with mannose-6-phosphate
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
3C0O 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
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