1YVG Hydrolase date Feb 15, 2005
title Structural Analysis Of The Catalytic Domain Of Tetanus Neurotoxin
authors K.N.Rao, D.Kumaran, T.Binz, S.Swaminathan
compound source
Molecule: Tetanus Toxin, Light Chain
Chain: A
Fragment: Chain L
Synonym: Tentoxylysin, Light Chain
Ec: 3.4.24.68
Engineered: Yes
Organism_scientific: Clostridium Tetani
Organism_common: Bacteria
Gene: Tetx
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
Expression_system_vector_type: Plasmid
symmetry Space Group: C 2 2 2
R_factor 0.218
crystal
cell
length a length b length c angle alpha angle beta angle gamma
106.610 177.280 54.550 90.00 90.00 90.00
method X-Ray Diffractionresolution 2.60 Å
ligand ZN enzyme Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA
related structures by homologous chain: 1Z7H
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 referenceStructural analysis of the catalytic domain of tetanus neurotoxin., Rao KN, Kumaran D, Binz T, Swaminathan S, Toxicon 2005 Jun 1;45(7):929-39. Epub 2005 Apr 13. PMID:15904688
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (71 Kb) [Save to disk]
  • Biological Unit Coordinates (1yvg.pdb1.gz) 134 Kb
  • CSU: Contacts of Structural Units for 1YVG
  • Likely Quarternary Molecular Structure file(s) for 1YVG
  • Structure Factors (152 Kb)
  • Retrieve 1YVG in mmCIF format [Save to disk]
  • View 1YVG in 3D
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  • Structure-derived information
  • Electron Density related parameters from EDS Electron Density Server, at Upsala
  • Dipole moment, from Dipole Server at Weizmann Institute
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  • Fold representative 1yvg from FSSP and Dali (Families of Structurally Similar Proteins)
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1yvg_A]
  • Other resources with information on 1YVG
  • InterPro: IPR006025 , IPR012500 , IPR011591 , IPR012928 , IPR000395
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