1YVG | Hydrolase | date | Feb 15, 2005 ![]() ![]() |
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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 |
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method | X-Ray Diffraction | resolution | 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 |
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Primary reference | Structural 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 |
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