Journal: EMBO Rep / Year: 2017 Title: The structure of the tetanus toxin reveals pH-mediated domain dynamics. Authors: Geoffrey Masuyer / Julian Conrad / Pål Stenmark / 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 ...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.
History
Deposition
Feb 12, 2017
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Header (metadata) release
Mar 29, 2017
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Map release
Jun 21, 2017
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Update
Nov 22, 2017
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Current status
Nov 22, 2017
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0.1) Details: The actual resolution of the cryo-EM map is lower than 4.5A, as the map suffers bias due to the preferred distribution of particle orientations. Number images used: 197000
Fitting was performed manually using the X-ray crystal structure of the Tetanus neurotoxin (PDB 5n0b) by docking the two domains (catalytic and translocation domains) expected to be a 'rigid body' and then refined using the 'Fit in Map' logarithm of the Chimera software. A similar approach was used to fit in the binding domain.
Refinement
Protocol: RIGID BODY FIT
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