1bov: Difference between revisions
New page: left|200px<br /><applet load="1bov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bov, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1bov.gif|left|200px]]<br /><applet load="1bov" size=" | [[Image:1bov.gif|left|200px]]<br /><applet load="1bov" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bov, resolution 2.2Å" /> | caption="1bov, resolution 2.2Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CELL-BINDING B OLIGOMER OF VEROTOXIN-1 FROM E. COLI'''<br /> | '''CRYSTAL STRUCTURE OF THE CELL-BINDING B OLIGOMER OF VEROTOXIN-1 FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
The Shiga toxin family, a group of cytotoxins associated with diarrhoeal | The Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins produced by enteropathogenic Escherichia coli. The family belongs to the A-B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect. | ||
==About this Structure== | ==About this Structure== | ||
1BOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1BOV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOV OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Read, R | [[Category: Read, R J.]] | ||
[[Category: Stein, P | [[Category: Stein, P E.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: toxin]] | [[Category: toxin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:30 2008'' | ||
Revision as of 09:57, 21 February 2008
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CRYSTAL STRUCTURE OF THE CELL-BINDING B OLIGOMER OF VEROTOXIN-1 FROM E. COLI
Overview
The Shiga toxin family, a group of cytotoxins associated with diarrhoeal diseases and the haemolytic uraemic syndrome, includes Shiga toxin from Shigella dysenteriae type 1 and verotoxins produced by enteropathogenic Escherichia coli. The family belongs to the A-B class of bacterial toxins, which includes the cholera toxin family, pertussis and diphtheria toxins. These toxins all have bipartite structures consisting of an enzymatic A subunit associated with a B oligomer which binds to specific cell-surface receptors, but their amino-acid sequences and pathogenic mechanisms differ. We have determined the crystal structure of the B oligomer of verotoxin-1 from E. coli. The structure unexpectedly resembles that of the B oligomer of the cholera toxin-like heat-labile enterotoxin from E. coli, despite the absence of detectable sequence similarity between these two proteins. This result implies a distant evolutionary relationship between the Shiga toxin and cholera toxin families. We suggest that the cell surface receptor-binding site lies in a cleft between adjacent subunits of the B pentamer, providing a potential target for drugs and vaccines to prevent toxin binding and effect.
About this Structure
1BOV is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli., Stein PE, Boodhoo A, Tyrrell GJ, Brunton JL, Read RJ, Nature. 1992 Feb 20;355(6362):748-50. PMID:1741063
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