PDBsum entry 5n0c

Toxin

PDB id: 5n0c

Contents

Protein chains

1293 a.a.

Ligands

BGC-GAL-NGA-GAL-SIA ×2

PEG

Metals

_ZN ×2

Waters ×452

PDB id:

5n0c

Name:

Toxin

Title:

Crystal structure of the tetanus neurotoxin in complex with gm1a

Structure:

Tetanus toxin. Chain: a, b. Synonym: tentoxylysin. Engineered: yes. Mutation: yes. Other_details: catalytically inactive variant of the tetanus neurotoxin. Missing residues could not be modelled due to lack of electron density.

Source:

Clostridium tetani. Organism_taxid: 1513. Gene: tetx, ctc_p60. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.60Å R-factor: 0.222 R-free: 0.253

Authors:

G.Masuyer,J.Conrad,P.Stenmark

Key ref:

G.Masuyer et al. (2017). The structure of the tetanus toxin reveals pH-mediated domain dynamics. EMBO Rep, 18, 1306-1317. PubMed id: 28645943

Date:

02-Feb-17 Release date: 21-Jun-17

Protein chains

P04958  (TETX_CLOTE) -  Tetanus toxin from Clostridium tetani (strain Massachusetts / E88)

Seq: 1315 a.a.

Struc: 1293 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.24.68 - tentoxilysin.
• Reaction: Hydrolysis of 76-Gln-|-Phe-77 bond in synaptobrevin 2.
• Cofactor: Zn(2+)

EMBO Rep 18:1306-1317 (2017)

PubMed id: 28645943

The structure of the tetanus toxin reveals pH-mediated domain dynamics.

G.Masuyer, J.Conrad, P.Stenmark.

ABSTRACT

The tetanus neurotoxin (TeNT) is a highly potent toxin produced byClostridium tetanithat 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.