1f82: Difference between revisions

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New page: left|200px<br /><applet load="1f82" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f82, resolution 2.20Å" /> '''BOTULINUM NEUROTOXIN...
 
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[[Image:1f82.jpg|left|200px]]<br /><applet load="1f82" size="450" color="white" frame="true" align="right" spinBox="true"
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'''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''<br />


==Overview==
==BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN==
Botulinum neurotoxin serotype B is a zinc protease that disrupts, neurotransmitter release by cleaving synaptobrevin-II (Sb2), one of three, SNARE proteins involved in neuronal synaptic vesicle fusion. The, three-dimensional crystal structure of the apo botulinum neurotoxin, serotype B catalytic domain (BoNT/B-LC) has been determined to 2.2 A, resolution, and the complex of cleaved Sb2 with the catalytic domain, (Sb2-BoNT/B-LC) has been determined to 2.0 A resolution. A comparison of, the holotoxin catalytic domain and the isolated BoNT/B-LC structure shows, a rearrangement of three active site loops. This rearrangement exposes the, BoNT/B active site. The Sb2-BoNT/B-LC structure illustrates two distinct, binding regions, which explains the specificity of each botulinum, neurotoxin for its synaptic vesicle protein. This observation provides an, explanation for the proposed cooperativity between binding of full-length, substrate and catalysis and suggest a mechanism of synaptobrevin, proteolysis employed by the clostridial neurotoxins.
<StructureSection load='1f82' size='340' side='right'caption='[[1f82]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f82]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F82 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f82 OCA], [https://pdbe.org/1f82 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f82 RCSB], [https://www.ebi.ac.uk/pdbsum/1f82 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f82 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BXB_CLOBO BXB_CLOBO] Botulinum 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 cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f8/1f82_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1f82 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F82 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F82 OCA].
*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution., Hanson MA, Stevens RC, Nat Struct Biol. 2000 Aug;7(8):687-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10932255 10932255]
[[Category: Bontoxilysin]]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hanson, M.A.]]
[[Category: Hanson MA]]
[[Category: Stevens, R.C.]]
[[Category: Stevens RC]]
[[Category: ZN]]
[[Category: botulinum neurotoxin]]
[[Category: zinc dependent protease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:41:53 2007''

Latest revision as of 10:11, 7 February 2024

BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAINBOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN

Structural highlights

1f82 is a 1 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BXB_CLOBO Botulinum 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 cleaves 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.

See Also

1f82, resolution 2.20Å

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