6H8P

JMJD2A/ KDM4A COMPLEXED WITH NI(II), NOG AND Histone H1.4(18-32)K26me3 peptide (15-mer)

Summary for 6H8P

• Entry DOI: 10.2210/pdb6h8p/pdb
• Descriptor: Lysine-specific demethylase 4A, Histone H1.4, NICKEL (II) ION, ... (8 entities in total)
• Functional Keywords: jmjd2a, kdm4a, oxidoreductase, non-heme, iron, 2-oxoglutarate, dioxygenase, oxygenase, double-stranded beta helix, dsbh, facial triad, demethylase, histone, jmjc domain, metal binding protein, epigenetic and transcription regulation, chromatin regulator, hydroxylation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 92812.16

Authors

Chowdhury, R.,Walport, L.J.,Schofield, C.J. (deposition date: 2018-08-03, release date: 2018-08-15, Last modification date: 2024-01-17)

Primary citation

Walport, L.J.,Hopkinson, R.J.,Chowdhury, R.,Zhang, Y.,Bonnici, J.,Schiller, R.,Kawamura, A.,Schofield, C.J.
Mechanistic and structural studies of KDM-catalysed demethylation of histone 1 isotype 4 at lysine 26.
FEBS Lett., 592:3264-3273, 2018

PubMed Abstract: N-Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)-catalysed demethylation of N -methylated lysine 26 on histone 1 isotype 4 (H1.4). The results reveal that methylated H1.4K26 is a substrate for all members of the KDM4 subfamily and that KDM4A-catalysed demethylation of H1.4K26me3 peptide is similarly efficient to that of H3K9me3. Crystallographic studies of an H1.4K26me3:KDM4A complex reveal a conserved binding geometry to that of H3K9me3. In the light of the high activity of the KDM4s on this mark, our results suggest JmjC KDM-catalysed demethylation of H1.4K26 may be as prevalent as demethylation on the H3 tail and warrants further investigation in cells.

PubMed: 30156264
DOI: 10.1002/1873-3468.13231

Experimental method

X-RAY DIFFRACTION (1.983 Å)