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 residues 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 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.

Sandbox Reserved 496: Difference between revisions

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Revision as of 00:23, 1 May 2012 view source Charlie Zogzas (talk \| contribs) 44 edits No edit summary ← Older edit		Revision as of 00:24, 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 residues 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 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.