1g9c: Difference between revisions

Revision as of 04:56, 1 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:1g9c.png

Template:STRUCTURE 1g9c

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 4)CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 4)

Template:ABSTRACT PUBMED 12146945

About this StructureAbout this Structure

1G9C is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

A novel mechanism for Clostridium botulinum neurotoxin inhibition., Eswaramoorthy S, Kumaran D, Swaminathan S, Biochemistry. 2002 Aug 6;41(31):9795-802. PMID:12146945

Page seeded by OCA on Tue Jul 1 04:56:12 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1g9c|  PDB=1g9c  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 4)'''
+===CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 4)===
-==Overview==
+<!--
-Clostridium botulinum neurotoxins are zinc endopeptidase proteins responsible for cleaving specific peptide bonds of proteins of neuroexocytosis apparatus. The ability of drugs to interfere with toxin's catalytic activity is being evaluated with zinc chelators and metalloprotease inhibitors. It is important to develop effective pharmacological treatment for the intact holotoxin before the catalytic domain separates and enters the cytosol. We present here evidence for a novel mechanism of an inhibitor binding to the holotoxin and for the chelation of zinc from our structural studies on Clostridium botulinum neurotoxin type B in complex with a potential metalloprotease inhibitor, bis(5-amidino-2-benzimidazolyl)methane, and provide snapshots of the reaction as it progresses. The binding and inhibition mechanism of this inhibitor to the neurotoxin seems to be unique for intact botulinum neurotoxins. The environment of the active site rearranges in the presence of the inhibitor, and the zinc ion is gradually removed from the active site and transported to a different site in the protein, probably causing loss of catalytic activity.
+The line below this paragraph, {{ABSTRACT_PUBMED_12146945}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12146945 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12146945}}
 ==About this Structure==
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 [[Category: Inhibitor]]
 [[Category: Neurotoxin]]
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