1f82

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[[Image:1f82.jpg|left|200px]]
 
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==BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1f82", creates the "Structure Box" on the page.
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<StructureSection load='1f82' size='340' side='right'caption='[[1f82]], [[Resolution|resolution]] 2.20&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'>[[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>
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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]] 2.2&#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_1f82| PDB=1f82 | 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=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>
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</table>
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== Function ==
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[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.
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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/f8/1f82_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=1f82 ConSurf].
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<div style="clear:both"></div>
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'''BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN'''
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==See Also==
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*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1F82 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10932255 10932255]
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[[Category: Bontoxilysin]]
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[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hanson, M A.]]
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[[Category: Hanson MA]]
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[[Category: Stevens, R C.]]
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[[Category: Stevens RC]]
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[[Category: Botulinum neurotoxin]]
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[[Category: Zinc dependent protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:00:52 2008''
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Current revision

BOTULINUM NEUROTOXIN TYPE B CATALYTIC DOMAIN

PDB ID 1f82

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