1s0g: Difference between revisions

Revision as of 00:32, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1s0g.png

Template:STRUCTURE 1s0g

Crystal structure of botulinum neurotoxin type B apo formCrystal structure of botulinum neurotoxin type B apo form

Template:ABSTRACT PUBMED 14979717

About this StructureAbout this Structure

1S0G is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 00:32:33 2008

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OCA

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-'''Crystal structure of botulinum neurotoxin type B apo form'''
+===Crystal structure of botulinum neurotoxin type B apo form===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14979717}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14979717 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14979717}}
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 [[Category: Neurotoxin]]
 [[Category: Ph]]
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