2nzg

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(New page: 200px<br /><applet load="2nzg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nzg, resolution 1.94&Aring;" /> '''Novel binding site i...)
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[[Image:2nzg.gif|left|200px]]<br /><applet load="2nzg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2nzg, resolution 1.94&Aring;" />
caption="2nzg, resolution 1.94&Aring;" />
'''Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details'''<br />
'''Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details'''<br />
==Overview==
==Overview==
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A hybrid between the B subunits of cholera toxin and Escherichia coli, heat-labile enterotoxin has been described, which exhibits a novel binding, specificity to blood group A and B type 2 determinants. In the present, investigation, we have determined the crystal structure of this protein, hybrid, termed LCTBK, in complex with the blood group A pentasaccharide, GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only, the novel binding specificity but also a distinct new oligosaccharide, binding site. Binding studies revealed that the new specificity can be, ascribed to a single mutation (S4N) introduced into the sequence of, Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the, new binding site is resolved in excellent detail. Main features include a, complex network of water molecules, which is well preserved by the parent, toxins, and an unexpectedly modest contribution to binding by the critical, residue Asn4, which interacts with the ligand only via a single water, molecule.
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A hybrid between the B subunits of cholera toxin and Escherichia coli heat-labile enterotoxin has been described, which exhibits a novel binding specificity to blood group A and B type 2 determinants. In the present investigation, we have determined the crystal structure of this protein hybrid, termed LCTBK, in complex with the blood group A pentasaccharide GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the novel binding specificity but also a distinct new oligosaccharide binding site. Binding studies revealed that the new specificity can be ascribed to a single mutation (S4N) introduced into the sequence of Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in excellent detail. Main features include a complex network of water molecules, which is well preserved by the parent toxins, and an unexpectedly modest contribution to binding by the critical residue Asn4, which interacts with the ligand only via a single water molecule.
==About this Structure==
==About this Structure==
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2NZG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. This structure superseeds the now removed PDB entry 1TL0. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NZG OCA].
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2NZG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. This structure supersedes the now removed PDB entry 1TL0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZG OCA].
==Reference==
==Reference==
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[[Category: protein-carbohydrate complex]]
[[Category: protein-carbohydrate complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:59:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:49 2008''

Revision as of 16:12, 21 February 2008


2nzg, resolution 1.94Å

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Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin, 1.9A crystal structure reveals the details

Overview

A hybrid between the B subunits of cholera toxin and Escherichia coli heat-labile enterotoxin has been described, which exhibits a novel binding specificity to blood group A and B type 2 determinants. In the present investigation, we have determined the crystal structure of this protein hybrid, termed LCTBK, in complex with the blood group A pentasaccharide GalNAcalpha3(Fucalpha2)Galbeta4(Fucalpha3)GlcNAcbeta, confirming not only the novel binding specificity but also a distinct new oligosaccharide binding site. Binding studies revealed that the new specificity can be ascribed to a single mutation (S4N) introduced into the sequence of Escherichia coli heat-labile enterotoxin. At a resolution of 1.9 A, the new binding site is resolved in excellent detail. Main features include a complex network of water molecules, which is well preserved by the parent toxins, and an unexpectedly modest contribution to binding by the critical residue Asn4, which interacts with the ligand only via a single water molecule.

About this Structure

2NZG is a Protein complex structure of sequences from Vibrio cholerae. This structure supersedes the now removed PDB entry 1TL0. Full crystallographic information is available from OCA.

Reference

Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details., Holmner A, Lebens M, Teneberg S, Angstrom J, Okvist M, Krengel U, Structure. 2004 Sep;12(9):1655-67. PMID:15341730

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