1zkk
From Proteopedia
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| - | [[Image:1zkk.gif|left|200px]] | + | [[Image:1zkk.gif|left|200px]] |
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| - | '''Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy''' | + | {{Structure |
| + | |PDB= 1zkk |SIZE=350|CAPTION= <scene name='initialview01'>1zkk</scene>, resolution 1.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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= SET8, PRSET7, SET07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZKK is a [ | + | 1ZKK 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=1ZKK OCA]. |
==Reference== | ==Reference== | ||
| - | Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase., Couture JF, Collazo E, Brunzelle JS, Trievel RC, Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. PMID:[http:// | + | Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase., Couture JF, Collazo E, Brunzelle JS, Trievel RC, Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15933070 15933070] |
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: pseudo-knot]] | [[Category: pseudo-knot]] | ||
| - | ''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 15:36:39 2008'' |
Revision as of 13:36, 20 March 2008
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| , resolution 1.45Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SET8, PRSET7, SET07 (Homo sapiens) | ||||||
| Activity: | Histone-lysine N-methyltransferase, with EC number 2.1.1.43 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy
Overview
SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific methyltransferase that is implicated in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. Herein we report the crystal structure of human SET8 (hSET8) bound to a histone H4 peptide bearing Lys-20 and the product cofactor S-adenosylhomocysteine. Histone H4 intercalates in the substrate-binding cleft as an extended parallel beta-strand. Residues preceding Lys-20 in H4 engage in an extensive array of salt bridge, hydrogen bond, and van der Waals interactions with hSET8, while the C-terminal residues bind through predominantly hydrophobic interactions. Mutational analysis of both the substrate-binding cleft and histone H4 reveals that interactions with residues in the N and C termini of the H4 peptide are critical for conferring substrate specificity. Finally, analysis of the product specificity indicates that hSET8 is a monomethylase, consistent with its role in the maintenance of Lys-20 monomethylation during cell division.
About this Structure
1ZKK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase., Couture JF, Collazo E, Brunzelle JS, Trievel RC, Genes Dev. 2005 Jun 15;19(12):1455-65. Epub 2005 Jun 2. PMID:15933070
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