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1yvg

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Revision as of 06:29, 25 April 2018

Structural analysis of the catalytic domain of tetanus neurotoxin

Structural highlights

1yvg is a 1 chain structure with sequence from "bacillus_tetani"_flugge_1886 "bacillus tetani" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	tetX ("Bacillus tetani" Flugge 1886)
Activity:	Tentoxilysin, with EC number 3.4.24.68
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rao KN, Kumaran D, Binz T, Swaminathan S. Structural analysis of the catalytic domain of tetanus neurotoxin. Toxicon. 2005 Jun 1;45(7):929-39. Epub 2005 Apr 13. PMID:15904688 doi:10.1016/j.toxicon.2005.02.032

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yvg"

@@ Line 1: / Line 1: @@
 ==Structural analysis of the catalytic domain of tetanus neurotoxin==
 <StructureSection load='1yvg' size='340' side='right' caption='[[1yvg]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tetX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1513 "Bacillus tetani" Flugge 1886])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvg OCA], [http://pdbe.org/1yvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yvg RCSB], [http://www.ebi.ac.uk/pdbsum/1yvg PDBsum]</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=1yvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yvg OCA], [http://pdbe.org/1yvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yvg RCSB], [http://www.ebi.ac.uk/pdbsum/1yvg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yvg ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yvg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yv/1yvg_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1yvg

From Proteopedia

Revision as of 06:29, 25 April 2018

Structural analysis of the catalytic domain of tetanus neurotoxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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