Sandbox GGC15: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

James Nolan, Student

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 == Active Site ==
-'''Topo 1 reduces stress in DNA by causing a transient single strand nick in the the DNA helix<ref name="Staker" />. This nick enables the cut to rotate around its intact complement, thus eliminating proximal supercoils<ref name="Staker" />.
+'''Topo 1 reduces stress in DNA by causing a transient single strand nick in the the DNA helix<ref name="Staker" />. This nick enables the cut to rotate around its intact complement, thus eliminating proximal supercoils<ref name="Staker" />.'''
-The active site of Topo 1 is catalytic and it is the location where the nicking or cutting occurs<ref name="Redinbo" />. The nicking occurs from the trans-esterification of Tyr-723 at a DNA phophodiester bond forming a  3'-phosphotyrosine covalent enzyme–DNA complex <ref name="Staker" />. After the DNA is relaxed, the covalent intermediate is reversed when the released  5'-OH of the broken strand reattacks the phosphotyrosine intermediate in a second transesterification reaction<ref name="Staker" />.
+The active site of Topo 1 is catalytic and it is the location where the nicking or cutting occurs<ref name="Redinbo" />. The nicking occurs from the trans-esterification of Tyr-723 at a DNA phophodiester bond forming a  3'-phosphotyrosine covalent enzyme–DNA complex <ref name="Staker" />. After the DNA is relaxed, the covalent intermediate is reversed when the released  5'-OH of the broken strand reattacks the phosphotyrosine intermediate in a second transesterification reaction<ref name="Staker" />.'''
 [[Image:4_27_21_1A36_Active_Site_Pict.jpg]]<ref name ="Stewart">Stewart, L. (1998). A Model for the Mechanism of Human Topoisomerase I. Science, 279(5356), 1534–1541. https://doi.org/10.1126/science.279.5356.1534</ref>
-'''
+[[Image:DNA and Tyrosine.jpg]]<ref name="Stewart" />