1A8D Neurotoxin date Mar 23, 1998
title Tetanus Toxin C Fragment
authors M.Knapp, B.Rupp
compound source
Molecule: Tetanus Neurotoxin
Chain: A
Fragment: C-Fragment
Ec: 3.4.24.68
Engineered: Yes
Mutation: Yes
Other_details: Gold (Au) Derivative
 Organism_scientific: Clostridium Tetani
Organism_common: Tetanus
Expression_system: Escherichia Coli
Other_details: Recombinant Protein, Purchased From Boehringer-Mannheim Catalog Number 1348-655
symmetry Space Group: P 21 21 21
R_factor
crystal
cell
length a length b length c angle alpha angle beta angle gamma
71.180 79.380 93.810 90.00 90.00 90.00
method X-Ray Diffractionresolution 1.57 Å
ligand AU enzyme Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
note 1A8D is a representative structure
related structures by homologous chain: 1DLL
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
    • Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (173 Kb) [Save to disk]
  • Biological Unit Coordinates (1a8d.pdb1.gz) 170 Kb
  • CSU: Contacts of Structural Units for 1A8D
  • Likely Quarternary Molecular Structure file(s) for 1A8D
  • Structure Factors (523 Kb)
  • Retrieve 1A8D in mmCIF format [Save to disk]
    • View 1A8D in 3D
  • Proteopedia, because life has more than 2D.
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    • Structure-derived information
  • Electron Density related parameters from EDS Electron Density Server, at Upsala
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  • 3D motif for 1A8D, from MSDmotif at EBI
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1a8d_1, region 1-247 [Jmol] [rasmolscript] [script source]
        - Domain d1a8d_2, region 248-452 [Jmol] [rasmolscript] [script source]
  • Fold representative 1a8d from FSSP and Dali (Families of Structurally Similar Proteins)
  • Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH
  • Summaries and structural analyses of PDB data files from PDBSum
  • Identification of Protein Pockets & Cavities at CASTp
    • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1a8d_A]
    • Other resources with information on 1A8D
  • InterPro: IPR006025 , IPR012500 , IPR011591 , IPR012928 , IPR000395
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  • MMDB (Entrez's Structure Database)
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