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1s0d

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Revision as of 07:04, 8 March 2018

Crystal structure of botulinum neurotoxin type B at pH 5.5

Structural highlights

1s0d is a 1 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1epw, 1g9a, 1s0b, 1s0c, 1s0e, 1s0f, 1s0g
Activity:	Bontoxilysin, with EC number 3.4.24.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Clostridium botulinum neurotoxins are the most potent toxins to humans and cause paralysis by blocking neurotransmitter release at the presynaptic nerve terminals. The toxicity involves four steps, viz., binding to neuronal cells, internalization, translocation, and catalytic activity. While the catalytic activity is a zinc endopeptidase activity on the SNARE complex proteins, the translocation is believed to be a pH-dependent process allowing the translocation domain to change its conformation to penetrate the endosomal membrane. Here, we report the crystal structures of botulinum neurotoxin type B at various pHs and of an apo form of the neurotoxin, and discuss the role of metal ions and the effect of pH variation in the biological activity. Except for the perturbation of a few side chains, the conformation of the catalytic domain is unchanged in the zinc-depleted apotoxin, suggesting that zinc's role is catalytic. We have also identified two calcium ions in the molecule and present biochemical evidence to show that they play a role in the translocation of the light chain through the membrane.

Role of metals in the biological activity of Clostridium botulinum neurotoxins.,Eswaramoorthy S, Kumaran D, Keller J, Swaminathan S Biochemistry. 2004 Mar 2;43(8):2209-16. PMID:14979717^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Eswaramoorthy S, Kumaran D, Keller J, Swaminathan S. Role of metals in the biological activity of Clostridium botulinum neurotoxins. Biochemistry. 2004 Mar 2;43(8):2209-16. PMID:14979717 doi:10.1021/bi035844k

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s0d"

@@ Line 1: / Line 1: @@
 ==Crystal structure of botulinum neurotoxin type B at pH 5.5==
 <StructureSection load='1s0d' size='340' side='right' caption='[[1s0d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1epw|1epw]], [[1g9a|1g9a]], [[1s0b|1s0b]], [[1s0c|1s0c]], [[1s0e|1s0e]], [[1s0f|1s0f]], [[1s0g|1s0g]]</td></tr>
 <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>
-<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=1s0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0d OCA], [http://pdbe.org/1s0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s0d RCSB], [http://www.ebi.ac.uk/pdbsum/1s0d PDBsum]</span></td></tr>
+<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=1s0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s0d OCA], [http://pdbe.org/1s0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s0d RCSB], [http://www.ebi.ac.uk/pdbsum/1s0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s0d ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s0/1s0d_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/s0/1s0d_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1s0d

From Proteopedia

Revision as of 07:04, 8 March 2018

Crystal structure of botulinum neurotoxin type B at pH 5.5

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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