User:Madeleine Wilson/Sandbox 1: Difference between revisions
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The <scene name='81/811091/C_terminal_domain/1'>C-terminal segment</scene> of lysine methyltransferase is essential for the catalytic activity of the enzyme. Hydrophobic packing of the C-terminal segment (residues 345-366) forms the lysine access channel. Residues 337-349 create a <scene name='81/811086/Beta_hairpin/2'>beta hairpin structure</scene> that stabilizes the orientation of two tyrosine residues Tyr 335 and Tyr337 that form the lysine access channel. The hydrophobic packing of the C-terminal <scene name='81/811091/C_terminal_domain/7'>alpha helix</scene> against beta sheet 19 (specifically residue 299) orient the SAM cofactor so the methyl donating group is oriented toward the lysine access channel. donating group is oriented toward the lysine access channel. | The <scene name='81/811091/C_terminal_domain/1'>C-terminal segment</scene> of lysine methyltransferase is essential for the catalytic activity of the enzyme. Hydrophobic packing of the C-terminal segment (residues 345-366) forms the lysine access channel. Residues 337-349 create a <scene name='81/811086/Beta_hairpin/2'>beta hairpin structure</scene> that stabilizes the orientation of two tyrosine residues Tyr 335 and Tyr337 that form the lysine access channel. The hydrophobic packing of the C-terminal <scene name='81/811091/C_terminal_domain/7'>alpha helix</scene> against beta sheet 19 (specifically residue 299) orient the SAM cofactor so the methyl donating group is oriented toward the lysine access channel. donating group is oriented toward the lysine access channel. | ||
The C-terminal domain of lysine methyltransferase is very important for the catalytic activity of the enzyme. The structures of the <scene name='81/811091/C_terminal_domain/1'>C-terminal domain (residues 345-366)</scene> serve the role of stabilizing the structures in the <scene name='81/811091/C_terminal_domain/16'>SET7 domain (residues 193-344)</scene> in the correct orientation for a reaction in the active site. | The C-terminal domain of lysine methyltransferase is very important for the catalytic activity of the enzyme. The structures of the <scene name='81/811091/C_terminal_domain/1'>C-terminal domain (residues 345-366)</scene> serve the role of stabilizing the structures in the <scene name='81/811091/C_terminal_domain/16'>SET7 domain (residues 193-344)</scene> in the correct orientation for a reaction in the active site.<ref name="Xiao" /> Hydrophobic interactions in the C-terminal domain are mainly responsible for stabilizing the access channel for the lysine methylation site on histone H3. Residues 337-349 create a beta-hairpin structure that stabilizes the orientation of two tyrosine residues, Tyr335 and Tyr337, that form the opening to the lysine access channel. Furthermore, the hydrophobic packing of alpha-helix 3 against beta-sheet 19, specifically <scene name='81/811091/C_terminal_domain/13'>residues Leu357 and Phe 299</scene>, stabilize the orientation of the <scene name='81/811091/C_terminal_domain/14'>SAM cofactor</scene> so that its methyl donating group is oriented toward the lysine access channel. The orientation of the SAM cofactor is further stabilized with its hydrophobic interactions with C-terminal domain residues <scene name='81/811091/C_terminal_domain/18'>Trp352 and Glu356</scene>. <ref name="Xiao" /> | ||
===The Active Site=== | ===The Active Site=== | ||
