User:Madeleine Wilson/Sandbox 1: Difference between revisions
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===The Active Site=== | ===The Active Site=== | ||
The active site and binding pocket of KMT have several essential characteristics for the overall efficiency. First, the lysine of the histone enters the active site via the | The active site and binding pocket of KMT have several essential characteristics for the overall efficiency. First, the lysine of the histone enters the active site via the <scene name='81/811092/Tyrosine_channel_2/3'>Lysine access channel</scene> comprised of Tyr335 and Tyr337. Once in the active site, the alkyl part of the histone chain is stabilized by the <scene name='81/811092/Hydrophobic_binding_pocket/1'>hydrophobic binding pocket</scene>, and polar residues are stabilized by hydrogen bonding interactions on the surface. The Tyr335 and Tyr337 are also essential for stabilization of histone chain via hydrogen bonding. | ||
The <scene name='81/811092/Active_site_w_water/2'>active site</scene> itself contains the cofactor S-adenosyl methionine (SAM) which donates the methyl group in the reaction. <ref name="Xiao" /> | The <scene name='81/811092/Active_site_w_water/2'>active site</scene> itself contains the cofactor S-adenosyl methionine (SAM) which donates the methyl group in the reaction. <ref name="Xiao" /> | ||
[[Image:KMT_mechanism.png|200px|left|thumb|KMT Mechanism]] | [[Image:KMT_mechanism.png|200px|left|thumb|KMT Mechanism]] | ||
