3bta
From Proteopedia
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|PDB= 3bta |SIZE=350|CAPTION= <scene name='initialview01'>3bta</scene>, resolution 3.2Å | |PDB= 3bta |SIZE=350|CAPTION= <scene name='initialview01'>3bta</scene>, resolution 3.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Lacy, D B.]] | [[Category: Lacy, D B.]] | ||
[[Category: Stevens, R C.]] | [[Category: Stevens, R C.]] | ||
| - | [[Category: ZN]] | ||
[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
[[Category: sugar binding protein]] | [[Category: sugar binding protein]] | ||
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[[Category: zinc protease]] | [[Category: zinc protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:47 2008'' |
Revision as of 02:28, 31 March 2008
| |||||||
| , resolution 3.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Bontoxilysin, with EC number 3.4.24.69 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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