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3bta

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[[Image:3bta.gif|left|200px]]
[[Image:3bta.gif|left|200px]]
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{{Structure
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|PDB= 3bta |SIZE=350|CAPTION= <scene name='initialview01'>3bta</scene>, resolution 3.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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{{STRUCTURE_3bta| PDB=3bta | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bta OCA], [http://www.ebi.ac.uk/pdbsum/3bta PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bta RCSB]</span>
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'''CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A'''
'''CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A'''
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[[Category: Lacy, D B.]]
[[Category: Lacy, D B.]]
[[Category: Stevens, R C.]]
[[Category: Stevens, R C.]]
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[[Category: neurotoxin]]
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[[Category: Neurotoxin]]
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[[Category: sugar binding protein]]
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[[Category: Sugar binding protein]]
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[[Category: translocation]]
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[[Category: Translocation]]
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[[Category: zinc protease]]
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[[Category: Zinc protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:04:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:47 2008''
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Revision as of 18:04, 4 May 2008

Image:3bta.gif

Template:STRUCTURE 3bta

CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A


Overview

Botulinum neurotoxin type A (BoNT/A) is the potent disease agent in botulism, a potential biological weapon and an effective therapeutic drug for involuntary muscle disorders. The crystal structure of the entire 1,285 amino acid di-chain neurotoxin was determined at 3.3 A resolution. The structure reveals that the translocation domain contains a central pair of alpha-helices 105 A long and a approximately 50 residue loop or belt that wraps around the catalytic domain. This belt partially occludes a large channel leading to a buried, negative active site--a feature that calls for radically different inhibitor design strategies from those currently used. The fold of the translocation domain suggests a mechanism of pore formation different from other toxins. Lastly, the toxin appears as a hybrid of varied structural motifs and suggests a modular assembly of functional subunits to yield pathogenesis.

About this Structure

3BTA is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

Reference

Crystal structure of botulinum neurotoxin type A and implications for toxicity., Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC, Nat Struct Biol. 1998 Oct;5(10):898-902. PMID:9783750 Page seeded by OCA on Sun May 4 21:04:53 2008

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