ATP-dependent DNA ligase from bacteriophage T7: Difference between revisions
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==Catalytic function with DNA== | ==Catalytic function with DNA== | ||
ATP-dependent DNA ligase from bacteriophage T7 amends a fractured DNA strand through esterification of a 5'- phosphoryl to a 3'- hydroxyl group. This mechanism occurs with the aid of ATP in several steps. First, the ligase is activated through a <scene name='56/567310/Amp_complex/1'>phosphoramidate bond with a lysine residue</scene> in the active site (Lys 34). A pyrophosphate leaves and the enzyme-AMP complex is formed. Next, the AMP is transferred to the 5' phosphate group at the nick in the DNA. Finally, T7 ligase creates the phosphodiester bond between the 5' -phosphoryl and the 3' – hydroxyl group, with AMP being freed. All ATP-dependent DNA ligases contain a conserved amino acid sequence of KxDGxR. This includes the lysine residue which binds the ATP in the groove between the two domains. | ATP-dependent DNA ligase from bacteriophage T7 amends a fractured DNA strand through esterification of a 5'- phosphoryl to a 3'- hydroxyl group. This mechanism occurs with the aid of ATP in several steps. First, the ligase is activated through a <scene name='56/567310/Amp_complex/1'>phosphoramidate bond with a lysine residue</scene> in the active site (Lys 34). A pyrophosphate leaves and the enzyme-AMP complex is formed. Next, the AMP is transferred to the 5' phosphate group at the nick in the DNA. Finally, T7 ligase creates the phosphodiester bond between the 5' -phosphoryl and the 3' – hydroxyl group, with AMP being freed. All ATP-dependent DNA ligases contain a conserved amino acid sequence of KxDGxR<ref>PMID: 8626651</ref>. This includes the lysine residue which binds the ATP in the groove between the two domains. | ||
</StructureSection> | </StructureSection> |