User:Wade Cook/Sandbox 1: Difference between revisions
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[[Image:Comparison_of_Euk_and_Viral_Topo.jpg ]] | [[Image:Comparison_of_Euk_and_Viral_Topo.jpg ]] | ||
In the above figure, [A] shows the C-terminal and N-terminal domains of eukaryotic topoisomerase 1B. [B] shows the C-terminal and N-terminal domains of viral topoisomerase 1B. Both domains are highly conserved between the different species, however, the N-terminal domain of viral topoisomerase 1B is slightly smaller and more simple than the larger eukaryotic N-terminal domain. The type 1B topoisomerase can relieve negative or positive supercoiling without the use of ATP. As long as there's torsional strain on the DNA strand from the supercoiling, this is enough potential energy to drive the uncoiling of the strand. Both eukaryotic and viral topoisomerase 1B enzymes contain a highly conserved active site consisting of five common amino acid residues. These residues are Tyr, Arg, Arg, Lys, His/Asp. | In the above figure, [A] shows the <scene name='71/716538/C-domain/1'>C-terminal</scene> and N-terminal domains of eukaryotic topoisomerase 1B. [B] shows the C-terminal and N-terminal domains of viral topoisomerase 1B. Both domains are highly conserved between the different species, however, the N-terminal domain of viral topoisomerase 1B is slightly smaller and more simple than the larger eukaryotic N-terminal domain. The type 1B topoisomerase can relieve negative or positive supercoiling without the use of ATP. As long as there's torsional strain on the DNA strand from the supercoiling, this is enough potential energy to drive the uncoiling of the strand. Both eukaryotic and viral topoisomerase 1B enzymes contain a highly conserved active site consisting of five common amino acid residues. These residues are Tyr, Arg, Arg, Lys, His/Asp. | ||
[[Image:Active_Sites_of_topo.jpg]] | [[Image:Active_Sites_of_topo.jpg]] | ||
