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1lta

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(New page: 200px<br /><applet load="1lta" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lta, resolution 2.2&Aring;" /> '''2.2 ANGSTROMS CRYSTAL...)
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[[Image:1lta.jpg|left|200px]]<br /><applet load="1lta" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lta, resolution 2.2&Aring;" />
caption="1lta, resolution 2.2&Aring;" />
'''2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE'''<br />
'''2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE'''<br />
==Overview==
==Overview==
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The galactose-binding site in cholera toxin and the closely related, heat-labile enterotoxin (LT) from Escherichia coli is an attractive target, for the rational design of potential anti-cholera drugs. In this paper we, analyse the molecular structure of this binding site as seen in several, crystal structures, including that of an LT:galactose complex which we, report here at 2.2 A resolution. The binding surface on the free toxin, contains several tightly associated water molecules and a relatively, flexible loop consisting of residues 51-60 of the B subunit. During, receptor binding this loop becomes tightly ordered by forming hydrogen, bonds jointly to the GM1 pentasaccharide and to a set of water molecules, which stabilize the toxin:receptor complex.
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The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex.
==About this Structure==
==About this Structure==
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1LTA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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=1LTA OCA].
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1LTA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] 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=1LTA OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hol, W G.J.]]
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[[Category: Kalk, K.H.]]
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[[Category: Kalk, K H.]]
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[[Category: Merritt, E.A.]]
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[[Category: Merritt, E A.]]
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[[Category: Sixma, T.K.]]
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[[Category: Sixma, T K.]]
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[[Category: Zanten, B.A.M.Van.]]
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[[Category: Zanten, B A.M Van.]]
[[Category: GAL]]
[[Category: GAL]]
[[Category: enterotoxin]]
[[Category: enterotoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:51:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:13 2008''

Revision as of 11:48, 21 February 2008


1lta, resolution 2.2Å

Drag the structure with the mouse to rotate

2.2 ANGSTROMS CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN (LT) WITH BOUND GALACTOSE

Overview

The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex.

About this Structure

1LTA is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT)., Merritt EA, Sixma TK, Kalk KH, van Zanten BA, Hol WG, Mol Microbiol. 1994 Aug;13(4):745-53. PMID:7997185

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