PMID:7997185
| Citation |
Merritt, EA, Sixma, TK, Kalk, KH, van Zanten, BA and Hol, WG (1994) Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol. Microbiol. 13:745-53 |
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| Abstract |
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. |
| Links | |
| Keywords |
Bacterial Toxins/chemistry; Bacterial Toxins/metabolism; Binding Sites; Calcium-Binding Proteins; Carbohydrate Sequence; Carrier Proteins/chemistry; Cholera Toxin/chemistry; Cholera Toxin/metabolism; Crystallography, X-Ray; Drug Design; Enterotoxins/chemistry; Enterotoxins/metabolism; Escherichia coli Proteins; Galactose/chemistry; Galactose/metabolism; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Monosaccharide Transport Proteins; Periplasmic Binding Proteins; Protein Conformation; Structure-Activity Relationship; Water/chemistry |
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