2a8a: Difference between revisions

Revision as of 19:42, 28 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:2a8a.png

Template:STRUCTURE 2a8a

Crystal structure of Clostridium botulinum neurotoxin serotype F light chainCrystal structure of Clostridium botulinum neurotoxin serotype F light chain

Template:ABSTRACT PUBMED 16128577

About this StructureAbout this Structure

2A8A is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design., Agarwal R, Binz T, Swaminathan S, Biochemistry. 2005 Sep 6;44(35):11758-65. PMID:16128577

Page seeded by OCA on Mon Jul 28 19:42:37 2008

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

OCA

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-[[Image:2a8a.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2a8a|  PDB=2a8a  |  SCENE=  }}
-'''Crystal structure of Clostridium botulinum neurotoxin serotype F light chain'''
+===Crystal structure of Clostridium botulinum neurotoxin serotype F light chain===
-==Overview==
+<!--
-The seven serologically distinct Clostridium botulinum neurotoxins (BoNTs A-G) are zinc endopeptidases which block the neurotransmitter release by cleaving one of the three proteins of the soluble N-ethylmaleimide-sensitive-factor attachment protein receptor complex (SNARE complex) essential for the fusion of vesicles containing neurotransmitters with target membranes. These metallopeptidases exhibit unique specificity for the substrates and peptide bonds they cleave. Development of countermeasures and therapeutics for BoNTs is a priority because of their extreme toxicity and potential misuse as biowarfare agents. Though they share sequence homology and structural similarity, the structural information on each one of them is required to understand the mechanism of action of all of them because of their specificity. Unraveling the mechanism will help in the ultimate goal of developing inhibitors as antibotulinum drugs for the toxins. Here, we report the high-resolution structure of active BoNT/F catalytic domain in two crystal forms. The structure was exploited for modeling the substrate binding and identifying the S1' subsite and the putative exosites which are different from BoNT/A or BoNT/B. The orientation of docking of the substrate at the active site is consistent with the experimental BoNT/A-LC:SNAP-25 peptide model and our proposed model for BoNT/E-LC:SNAP-25.
+The line below this paragraph, {{ABSTRACT_PUBMED_16128577}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16128577 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16128577}}
 ==About this Structure==
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 [[Category: X-ray]]
 [[Category: Zinc endopeptidase]]
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