2g7n: Difference between revisions

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==Structure of the Light Chain of Botulinum Neurotoxin Serotype A Bound to small Molecule Inhibitors==
==Structure of the Light Chain of Botulinum Neurotoxin Serotype A Bound to small Molecule Inhibitors==
<StructureSection load='2g7n' size='340' side='right' caption='[[2g7n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2g7n' size='340' side='right' caption='[[2g7n]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, atx, bna ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botA, atx, bna ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </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=2g7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g7n OCA], [http://pdbe.org/2g7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g7n RCSB], [http://www.ebi.ac.uk/pdbsum/2g7n 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=2g7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g7n OCA], [http://pdbe.org/2g7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g7n RCSB], [http://www.ebi.ac.uk/pdbsum/2g7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g7n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/2g7n_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/2g7n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 10:24, 20 June 2018

Structure of the Light Chain of Botulinum Neurotoxin Serotype A Bound to small Molecule InhibitorsStructure of the Light Chain of Botulinum Neurotoxin Serotype A Bound to small Molecule Inhibitors

Structural highlights

2g7n is a 1 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:botA, atx, bna ("Bacillus botulinus" van Ermengem 1896)
Activity:Bontoxilysin, with EC number 3.4.24.69
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BXA2_CLOBO] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of the three isoforms SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the '197-Gln-|-Arg-198' bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2g7n, resolution 1.90Å

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