3bta

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(New page: 200px<br /><applet load="3bta" size="450" color="white" frame="true" align="right" spinBox="true" caption="3bta, resolution 3.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:3bta.gif|left|200px]]<br /><applet load="3bta" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3bta, resolution 3.2&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A==
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Botulinum neurotoxin type A (BoNT/A) is the potent disease agent in, botulism, a potential biological weapon and an effective therapeutic drug, for involuntary muscle disorders. The crystal structure of the entire, 1,285 amino acid di-chain neurotoxin was determined at 3.3 A resolution., The structure reveals that the translocation domain contains a central, pair of alpha-helices 105 A long and a approximately 50 residue loop or, belt that wraps around the catalytic domain. This belt partially occludes, a large channel leading to a buried, negative active site--a feature that, calls for radically different inhibitor design strategies from those, currently used. The fold of the translocation domain suggests a mechanism, of pore formation different from other toxins. Lastly, the toxin appears, as a hybrid of varied structural motifs and suggests a modular assembly of, functional subunits to yield pathogenesis.
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<StructureSection load='3bta' size='340' side='right'caption='[[3bta]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3bta]] 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=3BTA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BTA 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]] 3.2&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bta OCA], [https://pdbe.org/3bta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bta RCSB], [https://www.ebi.ac.uk/pdbsum/3bta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bta ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BXA1_CLOBH BXA1_CLOBH] 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 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.
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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/bt/3bta_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3bta 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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Botulinum neurotoxin type A (BoNT/A) is the potent disease agent in botulism, a potential biological weapon and an effective therapeutic drug for involuntary muscle disorders. The crystal structure of the entire 1,285 amino acid di-chain neurotoxin was determined at 3.3 A resolution. The structure reveals that the translocation domain contains a central pair of alpha-helices 105 A long and a approximately 50 residue loop or belt that wraps around the catalytic domain. This belt partially occludes a large channel leading to a buried, negative active site--a feature that calls for radically different inhibitor design strategies from those currently used. The fold of the translocation domain suggests a mechanism of pore formation different from other toxins. Lastly, the toxin appears as a hybrid of varied structural motifs and suggests a modular assembly of functional subunits to yield pathogenesis.
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==About this Structure==
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Crystal structure of botulinum neurotoxin type A and implications for toxicity.,Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC Nat Struct Biol. 1998 Oct;5(10):898-902. PMID:9783750<ref>PMID:9783750</ref>
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3BTA 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=3BTA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of botulinum neurotoxin type A and implications for toxicity., Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC, Nat Struct Biol. 1998 Oct;5(10):898-902. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9783750 9783750]
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</div>
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[[Category: Bontoxilysin]]
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<div class="pdbe-citations 3bta" style="background-color:#fffaf0;"></div>
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[[Category: Clostridium botulinum]]
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[[Category: Single protein]]
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[[Category: Lacy, D.B.]]
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[[Category: Stevens, R.C.]]
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[[Category: ZN]]
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[[Category: neurotoxin]]
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[[Category: sugar binding protein]]
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[[Category: translocation]]
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[[Category: zinc protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:28:09 2007''
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==See Also==
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*[[Botulinum neurotoxin|Botulinum neurotoxin]]
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*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Clostridium botulinum]]
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[[Category: Large Structures]]
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[[Category: Lacy DB]]
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[[Category: Stevens RC]]

Current revision

CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A

PDB ID 3bta

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