1U2Z

Crystal structure of histone K79 methyltransferase Dot1p from yeast

Summary for 1U2Z

• Entry DOI: 10.2210/pdb1u2z/pdb
• Descriptor: Histone-lysine N-methyltransferase, H3 lysine-79 specific, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• Functional Keywords: histone methyltransferase, nucleosome, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: Q04089
• Total number of polymer chains: 3
• Total formula weight: 150855.48

Authors

Sawada, K.,Yang, Z.,Horton, J.R.,Collins, R.E.,Zhang, X.,Cheng, X. (deposition date: 2004-07-20, release date: 2004-09-07, Last modification date: 2024-03-13)

Primary citation

Sawada, K.,Yang, Z.,Horton, J.R.,Collins, R.E.,Zhang, X.,Cheng, X.
Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase
J.Biol.Chem., 279:43296-43306, 2004

PubMed Abstract: Methylation of Lys79 on histone H3 by Dot1p is important for gene silencing. The elongated structure of the conserved core of yeast Dot1p contains an N-terminal helical domain and a seven-stranded catalytic domain that harbors the binding site for the methyl-donor and an active site pocket sided with conserved hydrophobic residues. The S-adenosyl-L-homocysteine exhibits an extended conformation distinct from the folded conformation observed in structures of SET domain histone lysine methyltransferases. A catalytic asparagine (Asn479), located at the bottom of the active site pocket, suggests a mechanism similar to that employed for amino methylation in DNA and protein glutamine methylation. The acidic, concave cleft between the two domains contains two basic residue binding pockets that could accommodate the outwardly protruding basic side chains around Lys79 of histone H3 on the disk-like nucleosome surface. Biochemical studies suggest that recombinant Dot1 proteins are active on recombinant nucleosomes, free of any modifications.

PubMed: 15292170
DOI: 10.1074/jbc.M405902200

Experimental method

X-RAY DIFFRACTION (2.2 Å)