1h3i
From Proteopedia
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| - | [[Image:1h3i.jpg|left|200px]]<br /><applet load="1h3i" size=" | + | [[Image:1h3i.jpg|left|200px]]<br /><applet load="1h3i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h3i, resolution 2.10Å" /> | caption="1h3i, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9'''<br /> | '''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain A And B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1H3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A+And+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:52 2008'' |
Revision as of 07:45, 3 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
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