Sandbox Reserved 466

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{{Sandbox_Reserved_Robert_B_Rose_1}}
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== Introduction ==
== Introduction ==
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The tetanus toxin is produced by the bacteria ''Clostridium tetani''. Clostridium bacteria produces distinct neurotoxins that are extremely potent to humans.
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The tetanus toxin, or ''Clostridium tetani'', is produced by the bacteria Clostridium. Clostridium bacteria produces distinct neurotoxins that are extremely potent to humans. It releases two types of neurotoxins: "Clostridium botulinum" and "Clostridium tetani". It is part of the peptidase M27 family of proteins, which are metalloproteases. Metalloproteases bind with a divalent cation, usually zinc, which activates water molecules within the active site to hydrolyze peptide bonds.
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It is part of the peptidase M27 family of proteins. These proteins are a class of neurotoxins
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Clostridium tetani
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== Structure ==
== Structure ==
<Structure load='1YVG' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
<Structure load='1YVG' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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The Clostridium tetani precursor polypeptide is cleaved into a heavy and light chains. These two chains remain linked by a disulfide bridge. These chains are non-toxic when separated.

Revision as of 19:15, 26 April 2012

Contents

TETANUS TOXIN

This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500.
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Introduction

The tetanus toxin, or Clostridium tetani, is produced by the bacteria Clostridium. Clostridium bacteria produces distinct neurotoxins that are extremely potent to humans. It releases two types of neurotoxins: "Clostridium botulinum" and "Clostridium tetani". It is part of the peptidase M27 family of proteins, which are metalloproteases. Metalloproteases bind with a divalent cation, usually zinc, which activates water molecules within the active site to hydrolyze peptide bonds.

Clostridium tetani



Structure

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The Clostridium tetani precursor polypeptide is cleaved into a heavy and light chains. These two chains remain linked by a disulfide bridge. These chains are non-toxic when separated.



Mechanism of Action

Medical Implications or Possible Applications

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