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2.1.1.319: type I protein arginine methyltransferase

This is an abbreviated version!
For detailed information about type I protein arginine methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.319

Reaction

2 S-adenosyl-L-methionine +

[protein]-L-arginine
= 2 S-adenosyl-L-homocysteine +
[protein]-Nomega,Nomega-dimethyl-L-arginine

Synonyms

arginine methyltransferase 1, CARM1, coactivator-associated arginine methyltransferase 1, coactivator-associated arginine methyltransferase 1 variant 5, EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, Eucgr.C03665.1, PRMT I, PRMT-1, PRMT1, PRMT10, PRMT2, PRMT3, PRMT4, PRMT6, PRMT8, protein arginine methyltransferase 1, protein arginine methyltransferase 2, protein arginine methyltransferase 4, protein arginine methyltransferase 6, protein arginine methyltransferase I, protein arginine N-methyltransferase 2, protein arginine N-methyltransferase I, RMT1, Tb927.1.4690, Tb927.5.3960, type I protein arginine methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.319 type I protein arginine methyltransferase

Crystallization

Crystallization on EC 2.1.1.319 - type I protein arginine methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structure is solved and refined at 2.0 A resolution
cocrystallisations of the enzyme (CARM1(135-479)) with inhibitors are carried out in 24-well plates using the sitting-drop vapour diffusion method
sitting-drop vapor-diffusion method at 20°C. Six crystal structures of PRMT6 are solved and refined at 1.34 A for the highest resolution structure.The crystal structures reveal that the folding of the helix aX is required to stabilize a productive active site before methylation of the bound peptide can occur. In the absence of cofactor, metal cations can be found in the catalytic pocket at the expected position of the guanidinium moiety of the target arginine substrate
the structure is solved and refined at 2.0 A resolution