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Structure paper

TitleThe structure of the tetanus toxin reveals pH-mediated domain dynamics.
Journal, issue, pagesEMBO Rep, Vol. 18, Issue 8, Page 1306-1317, Year 2017
Publish dateJun 23, 2017
AuthorsGeoffrey Masuyer / Julian Conrad / Pål Stenmark /
PubMed AbstractThe tetanus neurotoxin (TeNT) is a highly potent toxin produced by that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. TeNT differs from the ...The tetanus neurotoxin (TeNT) is a highly potent toxin produced by that inhibits neurotransmission of inhibitory interneurons, causing spastic paralysis in the tetanus disease. TeNT differs from the other clostridial neurotoxins by its unique ability to target the central nervous system by retrograde axonal transport. The crystal structure of the tetanus toxin reveals a "closed" domain arrangement stabilised by two disulphide bridges, and the molecular details of the toxin's interaction with its polysaccharide receptor. An integrative analysis combining X-ray crystallography, solution scattering and single particle electron cryo-microscopy reveals pH-mediated domain rearrangements that may give TeNT the ability to adapt to the multiple environments encountered during intoxication, and facilitate binding to distinct receptors.
External linksEMBO Rep / PubMed:28645943 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.6 - 4.5 Å
Structure data

EMDB-3588:
Cryo-EM map of the tetanus neurotoxin
Method: EM (single particle) / Resolution: 4.5 Å

PDB-5n0b:
Crystal structure of the tetanus neurotoxin in complex with GD1a
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5n0c:
Crystal structure of the tetanus neurotoxin in complex with GM1a
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • clostridium tetani (bacteria)
KeywordsTOXIN / Tetanus neurotoxin / tetanospasmin / tentoxilysin / clostridial toxin

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