Sandbox WWC1: Difference between revisions

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== Background ==
== Background ==
Botulinum Toxin (BTX) is produced by three species of obligate anaerobe bacterium, primarily ''Clostridium botulism'', but ''Clostridium baratii'' and ''Clostridium butyricum'' also produce the protein <ref name="Hall"> PMID: 3988908</ref> <ref name="Aureli"> PMID: 3722863</ref> <ref>Arnon SS. Botulism as an intestinal toxemia. In: Blaser MJ, Smith PD, Ravdin JI, Greenberg HB, Guerrant RL, eds. Infections of the Gastrointestinal Tract. New York, NY: Raven Press; 1995:257-271.</ref>. ''Clostridium botulism'' is commonly found in soil, marine sediments, and the gut of grazing animals <ref name="Ward"> PMID: 5340653</ref> <ref name="Smith"> PMID: 355208</ref> <ref>Sugiyama H. Clostridium botulinum neurotoxin. Microbiol Rev. 1980;44:419–448. 28. Dodds KL. Clostridium botulinum in the environment. In: Hauschild AHW </ref> <ref>Dodds KL, eds. Clostridium botulinum—Ecology and Control in Foods. New York, NY: Marcel Dekker, Inc; 1992: 21–51. 29. </ref> <ref>Popoff MR. Ecology of neurotoxigenic strains of clostridia. In: Montecucco C, ed. Current Topics in Microbiology: Clostridial Neurotoxins. The Molecular Pathogenesis of Tetanus and Botulism. Vol 195. Berlin, Germany: Springer-Verlag; 1995: 1–29. </ref>  .BTX is only produced by these bacteria when there are anaerobic conditions that induce spore germination. Once produced, the protein can have toxic effects on animals and humans by causing botulism, a potentially fatal illness. BTX is also the active component of Botox.  
Botulinum Toxin (BTX) is produced by three species of obligate anaerobe bacterium, primarily ''Clostridium botulism'', but ''Clostridium baratii'' and ''Clostridium butyricum'' also produce the protein <ref name="Hall"> PMID: 3988908</ref> <ref name="Aureli"> PMID: 3722863</ref> <ref>Arnon SS. Botulism as an intestinal toxemia. In: Blaser MJ, Smith PD, Ravdin JI, Greenberg HB, Guerrant RL, eds. Infections of the Gastrointestinal Tract. New York, NY: Raven Press; 1995:257-271.</ref>. ''Clostridium botulism'' is commonly found in soil, marine sediments, and the gut of grazing animals <ref name="Ward"> PMID: 5340653</ref> <ref name="Smith"> PMID: 355208</ref> <ref>Sugiyama H. Clostridium botulinum neurotoxin. Microbiol Rev. 1980;44:419–448. 28. Dodds KL. Clostridium botulinum in the environment. In: Hauschild AHW </ref> <ref>Dodds KL, eds. Clostridium botulinum—Ecology and Control in Foods. New York, NY: Marcel Dekker, Inc; 1992: 21–51. 29. </ref> <ref name="Popoff"> PMID: 8542750</ref>  .BTX is only produced by these bacteria when there are anaerobic conditions that induce spore germination. Once produced, the protein can have toxic effects on animals and humans by causing botulism, a potentially fatal illness. BTX is also the active component of Botox.  
<Structure load='3BTA' size='350' frame='true' align='right' caption='Botulinum Toxin Neurotoxin Serotype A' scene='Insert optional scene name here' />
<Structure load='3BTA' size='350' frame='true' align='right' caption='Botulinum Toxin Neurotoxin Serotype A' scene='Insert optional scene name here' />


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94. </ref> <ref> Minton NP. 1995. Molecular genetics of
94. </ref> <ref> Minton NP. 1995. Molecular genetics of
clostridial neurotoxins. Curr. Top. Microbiol.
clostridial neurotoxins. Curr. Top. Microbiol.
Immunol. 195:161–94 </ref> <ref> Oguma K, Fujinaga Y, Inoue K. 1995.Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:161–68 </ref> <ref name="Lacy"> PMID: 10518945</ref> <refPopoff MR, Marvaud J-C. 1999. Structural and genomic features of clostridial neurotoxins. See Ref. 132, pp. 174–
Immunol. 195:161–94 </ref> <ref> Oguma K, Fujinaga Y, Inoue K. 1995.Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:161–68 </ref> <ref name="Lacy"> PMID: 10518945</ref> <ref name="Popoff" />).  
201 </ref>).  


The light chain contains the <scene name='69/696299/Consensus_sequence_heilh/1'>consensus sequence HELIH</scene> that codes for the binding of zinc, which subsequently regulates the endopeptidase activity of the light chain.  
The light chain contains the <scene name='69/696299/Consensus_sequence_heilh/1'>consensus sequence HELIH</scene> that codes for the binding of zinc, which subsequently regulates the endopeptidase activity of the light chain.