Literature summary for 3.4.24.68 extracted from

Chen, C.; Fu, Z.; Kim, J.J.; Barbieri, J.T.; Baldwin, M.R.
Gangliosides as high affinity receptors for tetanus neurotoxin (2009), J. Biol. Chem., 284, 26569-26577.

Search for more literature for 3.4.24.68

Crystallization (Commentary)

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

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

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 [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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Clostridium tetani	-	-	-

Posttranslational Modification

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 and Products (Substrate)

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

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

Synonyms	Comment	Organism
TeNT	-	Clostridium tetani
Tetanus neurotoxin	-	Clostridium tetani

General Information

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