1h3i

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[[Image:1h3i.jpg|left|200px]]
[[Image:1h3i.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1h3i |SIZE=350|CAPTION= <scene name='initialview01'>1h3i</scene>, resolution 2.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1h3i", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A+And+B'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1h3i| PDB=1h3i | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3i OCA], [http://www.ebi.ac.uk/pdbsum/1h3i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h3i RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9'''
'''CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9'''
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[[Category: Wilson, J R.]]
[[Category: Wilson, J R.]]
[[Category: Xiao, B.]]
[[Category: Xiao, B.]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:23:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:56 2008''
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Revision as of 15:23, 2 May 2008

Image:1h3i.jpg

Template:STRUCTURE 1h3i

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 Page seeded by OCA on Fri May 2 18:23:12 2008

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