1yvg

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[[Image:1yvg.gif|left|200px]]
 
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==Structural analysis of the catalytic domain of tetanus neurotoxin==
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The line below this paragraph, containing "STRUCTURE_1yvg", creates the "Structure Box" on the page.
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<StructureSection load='1yvg' size='340' side='right'caption='[[1yvg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1yvg]] 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=1YVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YVG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1yvg| PDB=1yvg | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvg OCA], [https://pdbe.org/1yvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yvg RCSB], [https://www.ebi.ac.uk/pdbsum/1yvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yvg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1yvg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Clostridium neurotoxins, comprising the tetanus neurotoxin and the seven antigenically distinct botulinum neurotoxins (BoNT/A-G), are among the known most potent bacterial protein toxins to humans. Although they have similar function, sequences and three-dimensional structures, the substrate specificity and the selectivity of peptide bond cleavage are different and unique. Tetanus and botulinum type B neurotoxins enzymatically cleave the same substrate, vesicle-associated membrane protein, at the same peptide bond though the optimum length of substrate peptide required for cleavage by them is different. Here, we present the first experimentally determined three-dimensional structure of the catalytic domain of tetanus neurotoxin and analyze its active site. The structure provides insight into the active site of tetanus toxin's proteolytic activity and the importance of the nucleophilic water and the role of the zinc ion. The probable reason for different modes of binding of vesicle-associated membrane protein to botulinum neurotoxin type B and the tetanus toxin is discussed. The structure provides a basis for designing a novel recombinant vaccine or structure-based drugs for tetanus.
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'''Structural analysis of the catalytic domain of tetanus neurotoxin'''
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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<ref>PMID:15904688</ref>
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==Overview==
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Clostridium neurotoxins, comprising the tetanus neurotoxin and the seven antigenically distinct botulinum neurotoxins (BoNT/A-G), are among the known most potent bacterial protein toxins to humans. Although they have similar function, sequences and three-dimensional structures, the substrate specificity and the selectivity of peptide bond cleavage are different and unique. Tetanus and botulinum type B neurotoxins enzymatically cleave the same substrate, vesicle-associated membrane protein, at the same peptide bond though the optimum length of substrate peptide required for cleavage by them is different. Here, we present the first experimentally determined three-dimensional structure of the catalytic domain of tetanus neurotoxin and analyze its active site. The structure provides insight into the active site of tetanus toxin's proteolytic activity and the importance of the nucleophilic water and the role of the zinc ion. The probable reason for different modes of binding of vesicle-associated membrane protein to botulinum neurotoxin type B and the tetanus toxin is discussed. The structure provides a basis for designing a novel recombinant vaccine or structure-based drugs for tetanus.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1YVG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YVG OCA].
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</div>
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<div class="pdbe-citations 1yvg" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15904688 15904688]
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*[[Tetanus toxin|Tetanus toxin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Clostridium tetani]]
[[Category: Clostridium tetani]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tentoxilysin]]
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[[Category: Binz T]]
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[[Category: Binz, T.]]
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[[Category: Kumaran D]]
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[[Category: Kumaran, D.]]
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[[Category: Rao KN]]
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[[Category: Rao, K N.]]
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[[Category: Swaminathan S]]
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[[Category: Swaminathan, S.]]
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[[Category: Clostridium neurotoxin]]
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[[Category: Hydrolase]]
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[[Category: Tetanus neurotoxin]]
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[[Category: Zinc metalloprotease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:36:19 2008''
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Current revision

Structural analysis of the catalytic domain of tetanus neurotoxin

PDB ID 1yvg

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