Lambda repressor: Difference between revisions

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==C-Terminal Domain (CTD)==

<StructureSection load='3bdn' size='350' side='left' caption='Dimerized CTDs of two cI monomers. Note ~~the~~ interactions between knotted β-sheets at the dimer-interface. Auto-cleavage active site residues are colored yellow. (PDB entry [[1F39]])' scene='Bacteriophage_Lambda_Repressor_cI/Ctd_dimer/1'>The CTD of Lambda Repressor assumes a structural conformation similar to a knotted β-sheet and is composed of 104 amino acid resides (residues 132-236). This conformation is key in establishing the homodimer-forming interaction with the CTD of the opposite monomer. The CTD also facilitates the dimer-dimer interaction necessary for cooperative-binding repression. The <scene name='Bacteriophage_Lambda_Repressor_cI/Cleavage_site_and_active_site/2'>active site</scene> of the auto-cleavage mechanism of Lambda Repressor is on the CTD. Two amino acid residues mediate the auto-cleavage activity of the repressor, Lys 192 and Ser 149 (Stayrook et. al 2008).</StructureSection>

<StructureSection load='3bdn' size='350' side='left' caption='Dimerized CTDs of two monomers. Note interactions between knotted β-sheets at the dimer-interface. Auto-cleavage active site residues are colored yellow. (PDB entry [[1F39]])' scene='Bacteriophage_Lambda_Repressor_cI/Ctd_dimer/1'>The CTD of Lambda Repressor assumes a structural conformation similar to a knotted β-sheet and is composed of 104 amino acid resides (residues 132-236). This conformation is key in establishing the homodimer-forming interaction with the CTD of the opposite monomer. The CTD also facilitates the dimer-dimer interaction necessary for cooperative-binding repression. The <scene name='Bacteriophage_Lambda_Repressor_cI/Cleavage_site_and_active_site/2'>active site</scene> of the auto-cleavage mechanism of Lambda Repressor is on the CTD. Two amino acid residues mediate the auto-cleavage activity of the repressor, Lys 192 and Ser 149 (Stayrook et. al 2008).</StructureSection>

Lambda repressor: Difference between revisions

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Revision as of 08:18, 27 November 2012 view source Wally Novak (talk \| contribs) 663 edits No edit summary ← Older edit		Revision as of 08:19, 27 November 2012 view source Wally Novak (talk \| contribs) 663 edits No edit summary Newer edit →
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	==C-Terminal Domain (CTD)==		==C-Terminal Domain (CTD)==

	<StructureSection load='3bdn' size='350' side='left' caption='Dimerized CTDs of two cI monomers. Note ~~the~~ interactions between knotted β-sheets at the dimer-interface. Auto-cleavage active site residues are colored yellow. (PDB entry [[1F39]])' scene='Bacteriophage_Lambda_Repressor_cI/Ctd_dimer/1'>The CTD of Lambda Repressor assumes a structural conformation similar to a knotted β-sheet and is composed of 104 amino acid resides (residues 132-236). This conformation is key in establishing the homodimer-forming interaction with the CTD of the opposite monomer. The CTD also facilitates the dimer-dimer interaction necessary for cooperative-binding repression. The <scene name='Bacteriophage_Lambda_Repressor_cI/Cleavage_site_and_active_site/2'>active site</scene> of the auto-cleavage mechanism of Lambda Repressor is on the CTD. Two amino acid residues mediate the auto-cleavage activity of the repressor, Lys 192 and Ser 149 (Stayrook et. al 2008).</StructureSection>		<StructureSection load='3bdn' size='350' side='left' caption='Dimerized CTDs of two monomers. Note interactions between knotted β-sheets at the dimer-interface. Auto-cleavage active site residues are colored yellow. (PDB entry [[1F39]])' scene='Bacteriophage_Lambda_Repressor_cI/Ctd_dimer/1'>The CTD of Lambda Repressor assumes a structural conformation similar to a knotted β-sheet and is composed of 104 amino acid resides (residues 132-236). This conformation is key in establishing the homodimer-forming interaction with the CTD of the opposite monomer. The CTD also facilitates the dimer-dimer interaction necessary for cooperative-binding repression. The <scene name='Bacteriophage_Lambda_Repressor_cI/Cleavage_site_and_active_site/2'>active site</scene> of the auto-cleavage mechanism of Lambda Repressor is on the CTD. Two amino acid residues mediate the auto-cleavage activity of the repressor, Lys 192 and Ser 149 (Stayrook et. al 2008).</StructureSection>