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spinqualitylabelsall models 1nw3, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the Catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase

Overview

Dot1 is an evolutionarily conserved histone methyltransferase that, methylates lysine-79 of histone H3 in the core domain. Unlike other, histone methyltransferases, Dot1 does not contain a SET domain, and it, specifically methylates nucleosomal histone H3. We have solved a 2.5 A, resolution structure of the catalytic domain of human Dot1, hDOT1L, in, complex with S-adenosyl-L-methionine (SAM). The structure reveals a unique, organization of a mainly alpha-helical N-terminal domain and a central, open alpha/beta structure, an active site consisting of a SAM binding, pocket, and a potential lysine binding channel. We also show that a, flexible, positively charged region at the C terminus of the catalytic, domain is critical for nucleosome binding and enzymatic activity. These, structural and biochemical analyses, combined with molecular modeling, provide mechanistic insights into the catalytic mechanism and nucleosomal, specificity of Dot1 proteins.

About this Structure

1NW3 is a Single protein structure of sequence from Homo sapiens with ACT, SO4 and SAM as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase., Min J, Feng Q, Li Z, Zhang Y, Xu RM, Cell. 2003 Mar 7;112(5):711-23. PMID:12628190

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