3efx | pdb_00003efx

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

spinqualitylabelsall models 3efx, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3efx is a 10 chain structure with sequence from Vibrio cholerae. This structure supersedes the now removed PDB entries 2nzg and 1tl0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.94Å Ligands: A2G, BGC, FUC, GAL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ELBH_ECOLX The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.CHTB_VIBCH The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cholera toxin 3D structures User:David Solfiell/sandbox 1

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