3B7B

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)

Summary for 3B7B

• Entry DOI: 10.2210/pdb3b7b/pdb
• Descriptor: Euchromatic histone-lysine N-methyltransferase 1, SULFATE ION (3 entities in total)
• Functional Keywords: ankyrin repeat, alternative splicing, ank repeat, chromatin regulator, methyltransferase, nucleus, phosphorylation, polymorphism, s-adenosyl-l-methionine, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9H9B1
• Total number of polymer chains: 2
• Total formula weight: 53119.80

Authors

Collins, R.E.,Horton, J.R.,Cheng, X. (deposition date: 2007-10-30, release date: 2008-02-12, Last modification date: 2024-04-03)

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)