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• W2072052008 abstract "Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 Å resolution structure of Rubisco large subunit methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine and a HEPES ion reveals an all-β architecture for the SET domain embedded within a larger α-helical enzyme fold. Conserved regions of the SET domain bind S-adenosylmethionine and substrate lysine at two sites connected by a pore. We propose that methyl transfer is catalyzed by a conserved Tyr at a narrow pore connecting the sites. The cofactor enters by a “back door” on the opposite side of the enzyme from substrate, promoting highly specific protein recognition and allowing addition of multiple methyl groups." @default.
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• W2072052008 date "2002-10-01" @default.
• W2072052008 modified "2023-10-14" @default.
• W2072052008 title "Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase" @default.
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• W2072052008 doi "https://doi.org/10.1016/s0092-8674(02)01000-0" @default.
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