1YXW
A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin
Summary for 1YXW
| Entry DOI | 10.2210/pdb1yxw/pdb |
| Related | 1AF9 |
| Descriptor | Tetanus toxin (Tentoxylysin), TYROSINE, GLUTAMIC ACID, ... (5 entities in total) |
| Functional Keywords | tetanus toxin, gd3, ganglioside, beta-trefoil, inhibitors, hydrolase |
| Biological source | Clostridium tetani |
| Total number of polymer chains | 1 |
| Total formula weight | 51009.46 |
| Authors | Jayaraman, S.,Eswaramoorthy, S.,Kumaran, D.,Swaminathan, S. (deposition date: 2005-02-22, release date: 2005-03-15, Last modification date: 2023-08-23) |
| Primary citation | Jayaraman, S.,Eswaramoorthy, S.,Kumaran, D.,Swaminathan, S. Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin Proteins, 61:288-295, 2005 Cited by PubMed Abstract: Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding. PubMed: 16104015DOI: 10.1002/prot.20595 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
