1h3i
From Proteopedia
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| - | [[Image:1h3i.jpg|left|200px]] | + | [[Image:1h3i.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9''' | + | {{Structure |
| + | |PDB= 1h3i |SIZE=350|CAPTION= <scene name='initialview01'>1h3i</scene>, resolution 2.10Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A+And+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H3I is a [ | + | 1H3I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3I OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12372304 12372304] |
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:31:43 2008'' |
Revision as of 09:31, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Histone-lysine N-methyltransferase, with EC number 2.1.1.43 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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