1lta
From Proteopedia
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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 GAL 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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