2nzg
From Proteopedia
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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 superseeds 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
Page seeded by OCA on Wed Nov 21 12:59:55 2007
