Crystallization (Comment) | Organism |
---|---|
purified C-terminal receptor binding domain with bound ganglioside GT2 in presence and absence of lactose, 10 mg/ml protein in 20 mM Tris-HCl buffer, pH 7.9, containing 100 mM NaCl are mixed with the carbohydrate moiety of GT2 at 1:8 molar ratio, vapor diffusion hanging drop method, 0.002 ml of protein-ligand solution are mixed with 0.002 ml of well solution containing 100 mM bis(trispropane) buffer, pH 7.0, 25% polyethylene glycol 2000 and 300 mM ammonium sulfate, equilibration against 0.5 ml well solution at 19°C, X-ray diffraction structure determination and analysis at 2.0-2.1 A resolution, molecular replacement method | Clostridium tetani |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of mutated forms of HCR/T that lack one or both carbohydrate-binding pocket, loss of gangliosides binding ability leads to loss of neuron binding ability of the toxin, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells, overview | Clostridium tetani |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain | Clostridium tetani |
100000 | - |
1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain | Clostridium tetani |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Clostridium tetani | TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview | ? | - |
? | |
vesicle-associated membrane protein-2 + H2O | Clostridium tetani | neuronal SNARE protein, i.e. VAMP2 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium tetani | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycolipoprotein | gangliosides are bound to the C-terminal receptor-binding domain via two carbohydrate-binding sites, termed the lactose-binding site or the W pocket, and the sialic acid-binding site or the R pocket, GM1a bound to the W pocket, and GD3 bound to the R pocket | Clostridium tetani |
proteolytic modification | TeNT is produced as a 150-kDa protein that is cleaved to a di-chain protein, comprising an N-terminal light chain and a C-terminal heavy chain domain linked through a single disulfide bond | Clostridium tetani |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | TeNT high affinity binding to neurons is mediated solely by its gangliosides, both of the W and R pockets are necessary for high affinity binding to neuronal and non-neuronal cells. Gangliosides are functional dual receptors for TeNT, overview | Clostridium tetani | ? | - |
? | |
vesicle-associated membrane protein-2 + H2O | neuronal SNARE protein, i.e. VAMP2 | Clostridium tetani | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 1 * 100000, C-terminal heavy chain, + 1 * 50000, N-terminal light chain | Clostridium tetani |
More | the TeNT heavy chain contains two functional domains: a translocation domain and a C-terminal receptor binding domain. C-terminal heavy and N-terminal light chains are linked through a single disulfide bond, overview | Clostridium tetani |
Synonyms | Comment | Organism |
---|---|---|
TeNT | - |
Clostridium tetani |
Tetanus neurotoxin | - |
Clostridium tetani |
General Information | Comment | Organism |
---|---|---|
malfunction | TeNT cleaves vesicle-associated membrane protein-2, thereby inhibiting neurotransmitter release in the central nervous system to elicit spastic paralysis | Clostridium tetani |