Sandbox Reserved 496: Difference between revisions

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== Cholix Toxin from ''Vibrio Cholerae ''==

The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the purified form of ''' Cholix Toxin''' or '''CT''' was determined in 1995.It is an oligomeric bacterial protein found to be made up of six individual subunits, one single α-subunit and 5 individual β- subunits.The α-subunit makes up what is known as the enzymatic portion of the protein while the 5 copies of the β-subunit are responsible for the binding to the ligand receptor. The toxin binds highly specifically and tightly to a [http://en.wikipedia.org/wiki/GM1_gangliosidoses GM1 gangliosides] on the surface of the host's cells. In this X-Ray Diffraction image we can see the <scene name='Sandbox_Reserved_496/Binding_site/1'>catalytic</scene> site, which in this case has been complexed with an allosteric inhibitor (red and yellow space filling atoms). Recent studies have indicated several amino acid <scene name='Sandbox_Reserved_496/Critical_amino_acids/2'> residues </scene> located proximally to the active site which are critical for enzymatic activity. Specifically, site directed mutagenesis indicated that when altered, the mutation results in a termination of the proteins toxicity, rendering it essentially harmless.

The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the purified form of ''' Cholix Toxin''' or '''CT''' was determined in 1995.It is an oligomeric bacterial protein found to be made up of six individual <scene name='Sandbox_Reserved_496/Secondary_structure/1'>subunits, </scene> one single α-subunit and 5 individual β- subunits.The α-subunit makes up what is known as the enzymatic portion of the protein while the 5 copies of the β-subunit are responsible for the binding to the ligand receptor. The toxin binds highly specifically and tightly to a [http://en.wikipedia.org/wiki/GM1_gangliosidoses GM1 gangliosides] on the surface of the host's cells. In this X-Ray Diffraction image we can see the <scene name='Sandbox_Reserved_496/Binding_site/1'>catalytic</scene> site, which in this case has been complexed with an allosteric inhibitor (red and yellow space filling atoms). Recent studies have indicated several amino acid <scene name='Sandbox_Reserved_496/Critical_amino_acids/2'> residues </scene> located proximally to the active site which are critical for enzymatic activity. Specifically, site directed mutagenesis indicated that when altered, the mutation results in a termination of the proteins toxicity, rendering it essentially harmless.

Sandbox Reserved 496: Difference between revisions

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Revision as of 00:24, 1 May 2012 view source Charlie Zogzas (talk \| contribs) 44 edits No edit summary ← Older edit		Revision as of 00:34, 1 May 2012 view source Charlie Zogzas (talk \| contribs) 44 edits No edit summary Newer edit →
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	== Cholix Toxin from ''Vibrio Cholerae ''==		== Cholix Toxin from ''Vibrio Cholerae ''==
	The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the purified form of ''' Cholix Toxin''' or '''CT''' was determined in 1995.It is an oligomeric bacterial protein found to be made up of six individual subunits, one single α-subunit and 5 individual β- subunits.The α-subunit makes up what is known as the enzymatic portion of the protein while the 5 copies of the β-subunit are responsible for the binding to the ligand receptor. The toxin binds highly specifically and tightly to a [http://en.wikipedia.org/wiki/GM1_gangliosidoses GM1 gangliosides] on the surface of the host's cells. In this X-Ray Diffraction image we can see the <scene name='Sandbox_Reserved_496/Binding_site/1'>catalytic</scene> site, which in this case has been complexed with an allosteric inhibitor (red and yellow space filling atoms). Recent studies have indicated several amino acid <scene name='Sandbox_Reserved_496/Critical_amino_acids/2'> residues </scene> located proximally to the active site which are critical for enzymatic activity. Specifically, site directed mutagenesis indicated that when altered, the mutation results in a termination of the proteins toxicity, rendering it essentially harmless.		The [http://en.wikipedia.org/wiki/Crystal_structure crystal structure] of the purified form of ''' Cholix Toxin''' or '''CT''' was determined in 1995.It is an oligomeric bacterial protein found to be made up of six individual <scene name='Sandbox_Reserved_496/Secondary_structure/1'>subunits, </scene> one single α-subunit and 5 individual β- subunits.The α-subunit makes up what is known as the enzymatic portion of the protein while the 5 copies of the β-subunit are responsible for the binding to the ligand receptor. The toxin binds highly specifically and tightly to a [http://en.wikipedia.org/wiki/GM1_gangliosidoses GM1 gangliosides] on the surface of the host's cells. In this X-Ray Diffraction image we can see the <scene name='Sandbox_Reserved_496/Binding_site/1'>catalytic</scene> site, which in this case has been complexed with an allosteric inhibitor (red and yellow space filling atoms). Recent studies have indicated several amino acid <scene name='Sandbox_Reserved_496/Critical_amino_acids/2'> residues </scene> located proximally to the active site which are critical for enzymatic activity. Specifically, site directed mutagenesis indicated that when altered, the mutation results in a termination of the proteins toxicity, rendering it essentially harmless.