1DFQ Toxin date Nov 20, 1999
title The Hc Fragment Of Tetanus Toxin Complexed With Sialic Acid
authors P.Emsley, C.Fotinou, I.Black, N.F.Fairweather, I.G.Charles, C.Watts, E.Hewitt, N.W.Isaacs
compound source
Molecule: Tetanus Toxin Hc
Chain: A
Fragment: C-Terminal Domain Of Heavy Chain
Ec: 3.4.24.68
Engineered: Yes
 Organism_scientific: Clostridium Tetani
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
Expression_system_plasmid: Pet16b
symmetry Space Group: P 21 21 21
R_factor 0.200
crystal
cell
length a length b length c angle alpha angle beta angle gamma
66.860 70.240 122.520 90.00 90.00 90.00
method X-Ray Diffractionresolution 2.60 Å
ligand SLB enzyme Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
related structures by homologous chain: 1AF9, 1FV2
similarity Belongs to the peptidase m27 family.[Toxin_trans]
subunit The precursor polypeptide is subsequently cleaved to yield subchains l and h. These remain linked by a disulfide bridge and are non-toxic after separation.
catalytic activ. Hydrolysis of 76-gln-|-phe-77 bond in synaptobrevin 2.
Gene CTC ; TETX (C. tetani)
function It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. Tetanus toxin acts by inhibiting neurotransmitter release. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the 76-gln-|-phe-77 bond of synaptobrevin-2.
Gene
Ontology
ChainFunctionProcessComponent
A
  • metalloendopeptidase activit...
  • peptidase activity
  • metallopeptidase activity
  • zinc ion binding
  • hydrolase activity
  • metal ion binding
  • proteolysis
  • pathogenesis
  • extracellular region
    • Primary referenceThe structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding., Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW, J Biol Chem 2000 Mar 24;275(12):8889-94. PMID:10722735
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (81 Kb) [Save to disk]
  • Biological Unit Coordinates (1dfq.pdb1.gz) 78 Kb
  • CSU: Contacts of Structural Units for 1DFQ
  • Likely Quarternary Molecular Structure file(s) for 1DFQ
  • Structure Factors (123 Kb)
  • Retrieve 1DFQ in mmCIF format [Save to disk]
    • View 1DFQ in 3D
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  • 3D motif for 1DFQ, from MSDmotif at EBI
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1dfqa2, region A:1111-1315 [Jmol] [rasmolscript] [script source]
        - Domain d1dfqa1, region A:875-1110 [Jmol] [rasmolscript] [script source]
  • Fold representative 1dfq from FSSP and Dali (Families of Structurally Similar Proteins)
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    • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1dfq_A]
    • Other resources with information on 1DFQ
  • InterPro: IPR006025 , IPR012500 , IPR011591 , IPR012928 , IPR000395
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