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 3.2Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 17:21, 20 November 2007
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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 ZN 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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