1H3I

Crystal structure of the Histone Methyltransferase SET7/9

Summary for 1H3I

• Entry DOI: 10.2210/pdb1h3i/pdb
• Descriptor: HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: transferase, methyltransferase
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus: Q8WTS6
• Total number of polymer chains: 2
• Total formula weight: 65216.74

Authors

Wilson, J.R.,Jing, C.,Walker, P.A.,Martin, S.R.,Howell, S.A.,Blackburn, G.M.,Gamblin, S.J.,Xiao, B. (deposition date: 2002-09-04, release date: 2002-11-11, Last modification date: 2024-05-08)

Primary citation

Wilson, J.R.,Jing, C.,Walker, P.A.,Martin, S.R.,Howell, S.A.,Blackburn, G.M.,Gamblin, S.J.,Xiao, B.
Crystal Structure and Functional Analysis of the Histone Methyltransferase Set7/9
Cell(Cambridge,Mass.), 111:105-, 2002

PubMed Abstract: Methylation of lysine residues in the N-terminal tails of histones is thought to represent an important component of the mechanism that regulates chromatin structure. The evolutionarily conserved SET domain occurs in most proteins known to possess histone lysine methyltransferase activity. We present here the crystal structure of a large fragment of human SET7/9 that contains a N-terminal beta-sheet domain as well as the conserved SET domain. Mutagenesis identifies two residues in the C terminus of the protein that appear essential for catalytic activity toward lysine-4 of histone H3. Furthermore, we show how the cofactor AdoMet binds to this domain and present biochemical data supporting the role of invariant residues in catalysis, binding of AdoMet, and interactions with the peptide substrate.

PubMed: 12372304
DOI: 10.1016/S0092-8674(02)00964-9

Experimental method

X-RAY DIFFRACTION (2.1 Å)