3bta

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(New page: 200px<br /><applet load="3bta" size="450" color="white" frame="true" align="right" spinBox="true" caption="3bta, resolution 3.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:3bta.gif|left|200px]]<br /><applet load="3bta" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3bta, resolution 3.2&Aring;" />
caption="3bta, resolution 3.2&Aring;" />
'''CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A'''<br />
'''CRYSTAL STRUCTURE OF BOTULINUM NEUROTOXIN SEROTYPE A'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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3BTA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3BTA OCA].
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3BTA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BTA OCA].
==Reference==
==Reference==
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[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lacy, D.B.]]
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[[Category: Lacy, D B.]]
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[[Category: Stevens, R.C.]]
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[[Category: Stevens, R C.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: neurotoxin]]
[[Category: neurotoxin]]
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[[Category: zinc protease]]
[[Category: zinc protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:28:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:07:26 2008''

Revision as of 17:07, 21 February 2008


3bta, resolution 3.2Å

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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 with as ligand. Active as Bontoxilysin, with EC number 3.4.24.69 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

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