5N0B

Crystal structure of the tetanus neurotoxin in complex with GD1a

Summary for 5N0B

• Entry DOI: 10.2210/pdb5n0b/pdb
• Descriptor: Tetanus toxin, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ZINC ION, ... (5 entities in total)
• Functional Keywords: tetanus neurotoxin, tetanospasmin, tentoxilysin, clostridial toxin, toxin
• Biological source: Clostridium tetani
• Total number of polymer chains: 1
• Total formula weight: 154371.50

Authors

Masuyer, G.,Conrad, J.,Stenmark, P. (deposition date: 2017-02-02, release date: 2017-06-21, Last modification date: 2024-11-06)

Primary citation

Masuyer, G.,Conrad, J.,Stenmark, P.
The structure of the tetanus toxin reveals pH-mediated domain dynamics.
EMBO Rep., 18:1306-1317, 2017

PubMed Abstract: 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.

PubMed: 28645943
DOI: 10.15252/embr.201744198

Experimental method

X-RAY DIFFRACTION (2.6 Å)