1YXW | Hydrolase | date | Feb 22, 2005 ![]() ![]() |
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title | A Common Binding Site For Disialyllactose And A Tri-Peptide In The C-Fragment Of Tetanus Neurotoxin | ||||||||||||||
authors | S.Jayaraman, S.Eswaramoorthy, D.Kumaran, S.Swaminathan | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Tetanus Toxin (Tentoxylysin) Chain: A Ec: 3.4.24.68 Other_details: Chain B Is Composed Of The Tri-Peptide Try- Glu-Trp |
Organism_scientific: Clostridium Tetani Organism_common: Bacteria | ||||||||||||||
symmetry | Space Group: P 21 21 21 | R_factor | 0.224 | ||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 2.20 Å | ||||||||||||
ligand | GLU, TRP, TYR | enzyme | Tentoxilysin;. Tetanus neurotoxin. Hydrolase E.C.3.4.24.68 BRENDA | ||||||||||||
related structures | by homologous chain: 1D0H, 1FV3 | ||||||||||||||
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 | Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin., Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S, Proteins 2005 Aug 15;. PMID:16104015 |
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