1z0h
From Proteopedia
(Difference between revisions)
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<StructureSection load='1z0h' size='340' side='right'caption='[[1z0h]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1z0h' size='340' side='right'caption='[[1z0h]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1z0h]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1z0h]] 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=1Z0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z0H FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1z0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0h OCA], [https://pdbe.org/1z0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z0h RCSB], [https://www.ebi.ac.uk/pdbsum/1z0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0h ProSAT]</span></td></tr> | |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Bacillus botulinus van ermengem 1896]] | ||
- | [[Category: Bontoxilysin]] | ||
- | [[Category: Large Structures]] | ||
- | [[Category: Ashraf, S A]] | ||
- | [[Category: Eswarmoorthy, S]] | ||
- | [[Category: Jayaraman, S]] | ||
- | [[Category: Smith, L A]] | ||
- | [[Category: Swaminathan, S]] | ||
- | [[Category: Binding domain]] | ||
[[Category: Clostridium botulinum]] | [[Category: Clostridium botulinum]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Ashraf SA]] |
+ | [[Category: Eswarmoorthy S]] | ||
+ | [[Category: Jayaraman S]] | ||
+ | [[Category: Smith LA]] | ||
+ | [[Category: Swaminathan S]] |
Current revision
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B
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