5mk7

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==Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 2)==
==Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 2)==
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<StructureSection load='5mk7' size='340' side='right' caption='[[5mk7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5mk7' size='340' side='right'caption='[[5mk7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5mk7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MK7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MK7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5mk7]] 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=5MK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MK7 FirstGlance]. <br>
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</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>
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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]] 1.8&#8491;</td></tr>
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<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>
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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=5mk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mk7 OCA], [https://pdbe.org/5mk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mk7 RCSB], [https://www.ebi.ac.uk/pdbsum/5mk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mk7 ProSAT]</span></td></tr>
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<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=5mk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mk7 OCA], [http://pdbe.org/5mk7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mk7 RCSB], [http://www.ebi.ac.uk/pdbsum/5mk7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mk7 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BXA1_CLOBO BXA1_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 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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[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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Botulinum neurotoxin|Botulinum neurotoxin]]
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*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus botulinus van ermengem 1896]]
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[[Category: Clostridium botulinum]]
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[[Category: Bontoxilysin]]
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[[Category: Large Structures]]
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[[Category: Acharya, K R]]
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[[Category: Acharya KR]]
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[[Category: Davies, J R]]
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[[Category: Davies JR]]
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[[Category: Bacterial]]
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[[Category: Beta trefoil fold]]
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[[Category: Jelly roll fold]]
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[[Category: Toxin]]
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[[Category: Toxin receptor binding domain]]
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Current revision

Crystal structure of the receptor-binding domain of botulinum neurotoxin A1 (crystal form 2)

PDB ID 5mk7

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