1bos

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(New page: 200px<br /><applet load="1bos" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bos, resolution 2.8&Aring;" /> '''SHIGA-LIKE TOXIN COMP...)
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caption="1bos, resolution 2.8&Aring;" />
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'''SHIGA-LIKE TOXIN COMPLEXED WITH ITS RECEPTOR'''<br />
'''SHIGA-LIKE TOXIN COMPLEXED WITH ITS RECEPTOR'''<br />
==Overview==
==Overview==
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Shiga-like toxin I (SLT-I) is a virulence factor of Escherichia coli, strains that cause disease in humans. Like other members of the Shiga, toxin family, it consists of an enzymatic (A) subunit and five copies of a, binding subunit (the B-pentamer). The B-pentamer binds to a specific, glycolipid, globotriaosylceramide (Gb3), on the surface of target cells, and thereby plays a crucial role in the entry of the toxin. Here we, present the crystal structure at 2.8 A resolution of the SLT-I B-pentamer, complexed with an analogue of the Gb3 trisaccharide. The structure reveals, a surprising density of binding sites, with three trisaccharide molecules, bound to each B-subunit monomer of 69 residues. All 15 trisaccharides bind, to one side of the B-pentamer, providing further evidence that this side, faces the cell membrane. The structural model is consistent with data from, site-directed mutagenesis and binding of carbohydrate analogues, and, allows the rational design of therapeutic Gb3 analogues that block the, attachment of toxin to cells.
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Shiga-like toxin I (SLT-I) is a virulence factor of Escherichia coli strains that cause disease in humans. Like other members of the Shiga toxin family, it consists of an enzymatic (A) subunit and five copies of a binding subunit (the B-pentamer). The B-pentamer binds to a specific glycolipid, globotriaosylceramide (Gb3), on the surface of target cells and thereby plays a crucial role in the entry of the toxin. Here we present the crystal structure at 2.8 A resolution of the SLT-I B-pentamer complexed with an analogue of the Gb3 trisaccharide. The structure reveals a surprising density of binding sites, with three trisaccharide molecules bound to each B-subunit monomer of 69 residues. All 15 trisaccharides bind to one side of the B-pentamer, providing further evidence that this side faces the cell membrane. The structural model is consistent with data from site-directed mutagenesis and binding of carbohydrate analogues, and allows the rational design of therapeutic Gb3 analogues that block the attachment of toxin to cells.
==About this Structure==
==About this Structure==
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1BOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_h30,_bacteriophage_h19b Bacteriophage h30, bacteriophage h19b] with GAL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BOS OCA].
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1BOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_h30,_bacteriophage_h19b Bacteriophage h30, bacteriophage h19b] with <scene name='pdbligand=GAL:'>GAL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BOS OCA].
==Reference==
==Reference==
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[[Category: Bacteriophage h30, bacteriophage h19b]]
[[Category: Bacteriophage h30, bacteriophage h19b]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Armstrong, G.D.]]
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[[Category: Armstrong, G D.]]
[[Category: Boodhoo, A.]]
[[Category: Boodhoo, A.]]
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[[Category: Brunton, J.L.]]
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[[Category: Brunton, J L.]]
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[[Category: Cummings, M.D.]]
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[[Category: Cummings, M D.]]
[[Category: Hazes, B.]]
[[Category: Hazes, B.]]
[[Category: Ling, H.]]
[[Category: Ling, H.]]
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[[Category: Read, R.J.]]
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[[Category: Read, R J.]]
[[Category: GAL]]
[[Category: GAL]]
[[Category: ob-fold]]
[[Category: ob-fold]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:47:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:28 2008''

Revision as of 09:57, 21 February 2008


1bos, resolution 2.8Å

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SHIGA-LIKE TOXIN COMPLEXED WITH ITS RECEPTOR

Overview

Shiga-like toxin I (SLT-I) is a virulence factor of Escherichia coli strains that cause disease in humans. Like other members of the Shiga toxin family, it consists of an enzymatic (A) subunit and five copies of a binding subunit (the B-pentamer). The B-pentamer binds to a specific glycolipid, globotriaosylceramide (Gb3), on the surface of target cells and thereby plays a crucial role in the entry of the toxin. Here we present the crystal structure at 2.8 A resolution of the SLT-I B-pentamer complexed with an analogue of the Gb3 trisaccharide. The structure reveals a surprising density of binding sites, with three trisaccharide molecules bound to each B-subunit monomer of 69 residues. All 15 trisaccharides bind to one side of the B-pentamer, providing further evidence that this side faces the cell membrane. The structural model is consistent with data from site-directed mutagenesis and binding of carbohydrate analogues, and allows the rational design of therapeutic Gb3 analogues that block the attachment of toxin to cells.

About this Structure

1BOS is a Single protein structure of sequence from Bacteriophage h30, bacteriophage h19b with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3., Ling H, Boodhoo A, Hazes B, Cummings MD, Armstrong GD, Brunton JL, Read RJ, Biochemistry. 1998 Feb 17;37(7):1777-88. PMID:9485303

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