5N0B

Crystal structure of the tetanus neurotoxin in complex with GD1a

5N0B の概要

• エントリーDOI: 10.2210/pdb5n0b/pdb
• 分子名称: 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)
• 機能のキーワード: tetanus neurotoxin, tetanospasmin, tentoxilysin, clostridial toxin, toxin
• 由来する生物種: Clostridium tetani
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 154371.50

構造登録者

Masuyer, G.,Conrad, J.,Stenmark, P. (登録日: 2017-02-02, 公開日: 2017-06-21, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)