2v74

File:2v74.gif

spinqualitylabelsall models 2v74, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1), IN COMPLEX WITH S-ADENOSYL-HOMOCYSTEINE

OverviewOverview

Coactivator-associated arginine methyltransferase (CARM1) is a, transcriptional coactivator that methylates Arg17 and Arg26 in histone H3., CARM1 contains a conserved protein arginine methyltransferase (PRMT), catalytic core flanked by unique pre- and post-core regions. The crystal, structures of the CARM1 catalytic core in the apo and holo states reveal, cofactor-dependent formation of a substrate-binding groove providing a, specific access channel for arginine to the active site. The groove is, supported by the first eight residues of the post-core region, (C-extension), not present in other PRMTs. In vitro methylation assays, show that the C-extension is essential for all histone H3 methylation, activity, whereas the pre-core region is required for methylation of, Arg26, but not Arg17. Kinetic analysis shows Arg17 methylation is, potentiated by pre-acetylation of Lys18, and this is reflected in k(cat), rather than K(m). Together with the absence of specificity subsites in the, structure, this suggests an electrostatic sensing mechanism for, communicating the modification status of vicinal residues as part of the, syntax of the 'histone code.'

About this StructureAbout this Structure

2V74 is a Single protein structure of sequence from Mus musculus with SAH as ligand. Active as Histone-arginine N-methyltransferase, with EC number 2.1.1.125 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase., Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, EMBO J. 2007 Sep 20;. PMID:17882261

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