5jwj | pdb_00005jwj
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NMR solution structure of a thermophilic lysine methyl transferase from Sulfolobus islandicus
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Structural highlights
FunctionKMT_SULIR Catalyzes the methylation of lysine residues in target proteins, using S-adenosyl-L-methionine (SAM) as the methyl donor. Exhibits broad substrate specificity, being able to methylate the crenarchaeal chromatin protein Cren7 primarily at 'Lys-11', 'Lys-16' and 'Lys-31', as well as a number of recombinant Sulfolobus proteins in vitro. Methylates lysine residues in a rather sequence-independent manner.[1] References
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This page was last modified 06:01, 19 June 2024.