1LTA

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

Summary for 1LTA

• Entry DOI: 10.2210/pdb1lta/pdb
• Descriptor: HEAT-LABILE ENTEROTOXIN, SUBUNIT B, HEAT-LABILE ENTEROTOXIN, SUBUNIT A, beta-D-galactopyranose, ... (5 entities in total)
• Functional Keywords: enterotoxin
• Biological source: Escherichia coli; More
• Total number of polymer chains: 7
• Total formula weight: 87519.82

Authors

Merritt, E.A.,Sixma, T.K.,Kalk, K.H.,Van Zanten, B.A.M.,Hol, W.G.J. (deposition date: 1993-09-15, release date: 1994-01-31, Last modification date: 2020-07-29)

Primary citation

Merritt, E.A.,Sixma, T.K.,Kalk, K.H.,van Zanten, B.A.,Hol, W.G.
Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT).
Mol.Microbiol., 13:745-753, 1994

PubMed 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.

PubMed: 7997185
DOI: 10.1111/j.1365-2958.1994.tb00467.x

Experimental method

X-RAY DIFFRACTION (2.2 Å)