Reference: Trievel RC, et al. (2002) Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell 111(1):91-103

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Abstract


Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of Rubisco large subunit methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine and a HEPES ion reveals an all-beta architecture for the SET domain embedded within a larger alpha-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.

Reference Type
Journal Article | Research Support, U.S. Gov't, Non-P.H.S.
Authors
Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH
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