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3ffz

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==Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation==
==Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation==
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<StructureSection load='3ffz' size='340' side='right' caption='[[3ffz]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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<StructureSection load='3ffz' size='340' side='right'caption='[[3ffz]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ffz]] is a 2 chain structure with 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=3FFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FFZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ffz]] is a 2 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=3FFZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 2.65&#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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ffz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffz OCA], [http://pdbe.org/3ffz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ffz RCSB], [http://www.ebi.ac.uk/pdbsum/3ffz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffz ProSAT]</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=3ffz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffz OCA], [https://pdbe.org/3ffz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffz RCSB], [https://www.ebi.ac.uk/pdbsum/3ffz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BXE_CLOBO BXE_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 catalyzes the hydrolysis of the 180-Arg-|-Ile-181 bond in SNAP-25.
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[https://www.uniprot.org/uniprot/BXE_CLOBO BXE_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 catalyzes the hydrolysis of the 180-Arg-|-Ile-181 bond in SNAP-25.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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: Bontoxilysin]]
 
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: Eswaramoorthy, S]]
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[[Category: Large Structures]]
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[[Category: Kumaran, D]]
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[[Category: Eswaramoorthy S]]
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[[Category: Swaminathan, S]]
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[[Category: Kumaran D]]
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[[Category: Botulinum neurotoxin serotype e]]
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[[Category: Swaminathan S]]
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[[Category: Botulism]]
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[[Category: Domain organization]]
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[[Category: Endopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Neurotoxin]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Toxin]]
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[[Category: Translocation]]
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[[Category: Transmembrane]]
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[[Category: Zinc]]
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Current revision

Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation

PDB ID 3ffz

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