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1.14.11.69: [histone H3]-trimethyl-L-lysine36 demethylase

This is an abbreviated version!
For detailed information about [histone H3]-trimethyl-L-lysine36 demethylase, go to the full flat file.

Word Map on EC 1.14.11.69

Reaction

a [histone H3]-N6,N6,N6-trimethyl-L-lysine36
+ 2 2-oxoglutarate + 2 O2 =
a [histone H3]-N6-methyl-L-lysine36
 + 2 succinate + 2 formaldehyde + 2 CO2

Synonyms

AN1060, CG15835, CG33182, dKDM4A, Dmel\Kdm4A, DNA damage-responsive transcriptional repressor, H3K36 demethylase, H3K36 histone demethylase, H3K9/36me3 lysine demethylase, histone demethylase JmjD2A, histone H3 demethylase, histone H3K36 demethylase, histone H3K9/H3K36 trimethyldemethylase, histone lysine demethylase, JHDM3A, JHDM3B, JmjC demethylase, JmjC histone lysine demethylase, JmjC protein, JMJD-2, JMJD2A, JMJD2A demethylase, JMJD2B, JMJD2C, jumonji domain containing 2A, JumonjiC-domain-containing histone demethylase, JumonjiD2A, KDM, KDM4, KDM4A, KDM4A demethylase, KDM4A lysine demethylase, KDM4A,, KDM4A/JMJD2A, KDM4B, Kdm4c, KdmA, LD33386, lysine trimethyl-specific JmjC histone demethylase, lysine-specific demethylase 4A, More, Rph1, Rph1/KDM4, trimethyllysine-specific histone demethylase, trimethyllysine-specific JmjC HDM

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.69 [histone H3]-trimethyl-L-lysine36 demethylase

Crystallization

Crystallization on EC 1.14.11.69 - [histone H3]-trimethyl-L-lysine36 demethylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determinations of JMJD2A in complex with histone H3 peptides bearing different methylated forms of K9 and K36
purified JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides, vapor diffusion method, from 0.2 M sodium/potassium phosphate, pH 6.5, and 20% w/v PEG 3350, at 4°C, and by microseeding from 12% w/v PEG monomethyl ether 5000 and 0.1 M HEPES, pH 7.0, X-ray diffraction structure determination and analysis at 2.05-2.30 A resolution
purified recombinant enzyme in complex with inhibitor, sitting drop vapor diffusion method, mixing of 7 mg/ml protein and 2 mM N-oxalylglycine with well solution, containing 25% v/v PEG 3350, 0.2 M sodium nitrate, 0.1 M bis-tris propane, pH 6.5, 5% v/v ethylene glycol, 0.01 M NiCl2, in a 2:1 ratio, 4°C, X-ray diffraction structure determination and analysis at 2.55 A resolution
purified recombinant enzyme in complex with substrate peptides, by vapour diffusion at 4°C from 0.1 M citrate, pH 5.5, 20% PEG 3350 and 4 mM NiCl2, X-ray diffraction structure determination and analysis at 2.1 A resolution
purified recombinant JMJD2A catalytic core complexed with methylated H3K36 peptide substrates (trimethylated H3K36 peptide (H3K36me3) or a monomethylated H3K36 peptide (H3K36me)) in the presence of Fe(II) and N-oxalylglycine, vapor diffusion method at 4°C against a solution containing 200 mM MgCl2, 100 mM Tris, pH 8.5, and 13-15% PEG 5000, X-ray diffraction structure determination and analysis at 2.0 A resolution
structures of the JMJD2A catalytic domain in complex with H3K9me3, H3K36me2 and H3K36me3 peptides. The histone substrates are recognized through a network of backbone hydrogen bonds and hydrophobic interactions that deposit the trimethyllysine into the active site. The trimethylated epsilon-ammonium cation is coordinated within a methylammonium-binding pocket through carbonoxygen hydrogen bonds that position one of the theta-methyl groups adjacent to the Fe(II) center for hydroxylation and demethylation
catalytic core of Rph1, hanging drop vapour diffusion method, X-ray diffraction structure determination and analysis at 2.5 A resolution