3B95

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)

Summary for 3B95

• Entry DOI: 10.2210/pdb3b95/pdb
• Related: 3B7B
• Descriptor: Euchromatic histone-lysine N-methyltransferase 1, Histone H3 N-terminal Peptide, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ankyrin repeat, ank repeat, methyltransferase, transferase, transferase-structural protein complex, transferase/structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 54904.77

Authors

Collins, R.E.,Horton, J.R.,Cheng, X. (deposition date: 2007-11-02, release date: 2008-02-12, Last modification date: 2023-08-30)

Primary citation

Collins, R.E.,Northrop, J.P.,Horton, J.R.,Lee, D.Y.,Zhang, X.,Stallcup, M.R.,Cheng, X.
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.
Nat.Struct.Mol.Biol., 15:245-250, 2008

PubMed Abstract: Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.

PubMed: 18264113
DOI: 10.1038/nsmb.1384

Experimental method

X-RAY DIFFRACTION (2.99 Å)