1bov

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(New page: 200px<br /><applet load="1bov" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bov, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1bov.gif|left|200px]]<br /><applet load="1bov" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bov.gif|left|200px]]<br /><applet load="1bov" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bov, resolution 2.2&Aring;" />
caption="1bov, resolution 2.2&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BOV OCA].
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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]]
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[[Category: Read, R.J.]]
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[[Category: Read, R J.]]
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[[Category: Stein, P.E.]]
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[[Category: Stein, P E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:48:08 2007''
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''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


1bov, resolution 2.2Å

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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 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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