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| | <StructureSection load='1yyn' size='340' side='right'caption='[[1yyn]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1yyn' size='340' side='right'caption='[[1yyn]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1yyn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tetani"_flugge_1886 "bacillus tetani" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YYN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1yyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YYN FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1af9|1af9]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyn OCA], [https://pdbe.org/1yyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yyn RCSB], [https://www.ebi.ac.uk/pdbsum/1yyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyn ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyn OCA], [http://pdbe.org/1yyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yyn RCSB], [http://www.ebi.ac.uk/pdbsum/1yyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TETX_CLOTE TETX_CLOTE]] Tetanus toxin acts by inhibiting neurotransmitter release. 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. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2. | + | [https://www.uniprot.org/uniprot/TETX_CLOTE TETX_CLOTE] Tetanus toxin acts by inhibiting neurotransmitter release. 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. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus tetani flugge 1886]] | + | [[Category: Clostridium tetani]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tentoxilysin]]
| + | [[Category: Eswaramoorthy S]] |
| - | [[Category: Eswaramoorthy, S]] | + | [[Category: Kumaran D]] |
| - | [[Category: Kumaran, D]] | + | [[Category: Seetharaman J]] |
| - | [[Category: Seetharaman, J]] | + | [[Category: Swaminathan S]] |
| - | [[Category: Swaminathan, S]] | + | |
| - | [[Category: Beta-trefoil]]
| + | |
| - | [[Category: Ganglioside]]
| + | |
| - | [[Category: Gd3]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Tetanus toxin]]
| + | |
| Structural highlights
Function
TETX_CLOTE Tetanus toxin acts by inhibiting neurotransmitter release. 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. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding.
Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin.,Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S Proteins. 2005 Nov 1;61(2):288-95. PMID:16104015[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S. Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin. Proteins. 2005 Nov 1;61(2):288-95. PMID:16104015 doi:10.1002/prot.20595
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