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

Journal article
Authors Åsa Holmner
Michael Lebens
Susann Teneberg
Jonas Ångström
Mats Ökvist
Ute Krengel
Published in Structure (London, England : 1993)
Volume 12
Issue 9
Pages 1655-67
ISSN 0969-2126
Publication year 2004
Published at Department of Chemistry
Institute of Medical Biochemistry
Institute of Medical Microbiology/Immunology
Pages 1655-67
Language en
Keywords Asparagine, metabolism, Bacterial Toxins, chemistry, genetics, metabolism, Binding Sites, Blood Group Antigens, metabolism, Cholera Toxin, chemistry, genetics, metabolism, Crystallography, X-Ray, Drug Design, Enterotoxins, chemistry, genetics, metabolism, Escherichia coli Proteins, chemistry, genetics, metabolism, Glycosphingolipids, chemistry, metabolism, Humans, Models, Molecular, Molecular Sequence Data, Molecular Structure, Oligosaccharides, chemistry, metabolism, Protein Binding, Protein Structure, Tertiary, Protein Subunits, chemistry, genetics, metabolism, Recombinant Fusion Proteins, chemistry, genetics, metabolism, Water, chemistry
Subject categories Medical and Health Sciences


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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