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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.357catalytic domain, in 0.2 M lithium sulfate, 0.1 M HEPES, pH 7.5, and 25% (w/v) PEG 3350 at 20°C
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.357molecular modelling of the open-and-closed conformation of the catalytic domain
Display the word mapDisplay the reaction diagram Show all sequences 2.1.1.357the SET domain is composed of three groups of canonical beta-sheets arranged in a triangular fashion with a group of two beta-sheets closely neighboring a conserved alpha-helix defining a cleft for the binding to the histone-tail ligand. The cofactor AdoMet and substrate bind at two adjacent sites to the SET domain. The histone-tail ligand binds into a groove formed by both the SET and postSET domains. The cofactor AdoMet binds into a distinct pocket located on the other side of the SET domain and acts as a methyl group donor. Both AdoMet and the L-lysine-histone are connected through a narrow tunnel where the methyl group is channeled. In the structure of the peptide-less NSDx02SET domain, the postSET domain loop is extended on top of the histone binding site, which sterically prevents the binding of either H3K36 or H4K20 substrates. In the presence of ligand, a network of residues stabilizes the H4-peptide tail on the binding site
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