1h3i
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Methylation of lysine residues in the N-terminal tails of histones is | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blackburn, G | + | [[Category: Blackburn, G M.]] |
| - | [[Category: Gamblin, S | + | [[Category: Gamblin, S J.]] |
| - | [[Category: Howell, S | + | [[Category: Howell, S A.]] |
[[Category: Jing, C.]] | [[Category: Jing, C.]] | ||
| - | [[Category: Martin, S | + | [[Category: Martin, S R.]] |
| - | [[Category: Walker, P | + | [[Category: Walker, P A.]] |
| - | [[Category: Wilson, J | + | [[Category: Wilson, J R.]] |
[[Category: Xiao, B.]] | [[Category: Xiao, B.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:57:00 2008'' |
Revision as of 10:57, 21 February 2008
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CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9
Overview
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.
About this Structure
1H3I is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure and functional analysis of the histone methyltransferase SET7/9., Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, Blackburn GM, Gamblin SJ, Xiao B, Cell. 2002 Oct 4;111(1):105-15. PMID:12372304
Page seeded by OCA on Thu Feb 21 12:57:00 2008
