Editing Tetanus toxin (section)

== Structure ==
The tetanus toxin [[protein]] has a molecular weight of 150&nbsp;[[Atomic mass unit|kDa]]. It is translated from the ''tetX'' gene as one protein which is subsequently cleaved into two parts: a 100&nbsp;kDa heavy or B-chain and a 50&nbsp;kDa light or A-chain. The chains are connected by a [[Disulfide#Occurrence in proteins|disulfide bond]].
* The  B-chain binds to disialo[[ganglioside]]s (GD2 and GD1b) on the neuronal membrane and contains a translocation domain which aids the movement of the protein across that membrane and into the neuron.
* The A-chain, an M27-family zinc [[endopeptidase]], attacks the [[vesicle-associated membrane protein]] (VAMP).

The TetX gene encoding this protein is located on the PE88 plasmid.<ref>{{cite journal | vauthors = Eisel U, Jarausch W, Goretzki K, Henschen A, Engels J, Weller U, Hudel M, Habermann E, Niemann H | title = Tetanus toxin: primary structure, expression in E. coli, and homology with botulinum toxins | journal = The EMBO Journal | volume = 5 | issue = 10 | pages = 2495–2502 | date = October 1986 | pmid = 3536478 | pmc = 1167145 | doi = 10.1002/j.1460-2075.1986.tb04527.x }}</ref><ref name="Alp">{{cite journal | vauthors = Popp D, Narita A, Lee LJ, Ghoshdastider U, Xue B, Srinivasan R, Balasubramanian MK, Tanaka T, Robinson RC | title = Novel actin-like filament structure from Clostridium tetani | journal = The Journal of Biological Chemistry | volume = 287 | issue = 25 | pages = 21121–21129 | date = June 2012 | pmid = 22514279 | pmc = 3375535 | doi = 10.1074/jbc.M112.341016 | doi-access = free }}</ref>

Several structures of the binding domain and the peptidase domain have been solved by [[X-ray crystallography]] and deposited in the [[Protein Data Bank|PDB]].<ref>{{cite web | title = Advanced Search for UniProt ID P04958 | work = Protein Databank in Europe (PDBe) | url = https://www.ebi.ac.uk/pdbe/entry/search/index/index?uniprot:P04958 }}</ref>