1zkk
From Proteopedia
(New page: 200px<br /> <applet load="1zkk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zkk, resolution 1.45Å" /> '''Crystal structure o...) |
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| - | [[Image:1zkk.gif|left|200px]]<br /> | + | [[Image:1zkk.gif|left|200px]]<br /><applet load="1zkk" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1zkk" size=" | + | |
caption="1zkk, resolution 1.45Å" /> | caption="1zkk, resolution 1.45Å" /> | ||
'''Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy'''<br /> | '''Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific | + | 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== | ==About this Structure== | ||
| - | 1ZKK 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 SAH 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] Full crystallographic information is available from [http:// | + | 1ZKK 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=SAH:'>SAH</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunzelle, J | + | [[Category: Brunzelle, J S.]] |
[[Category: Collazo, E.]] | [[Category: Collazo, E.]] | ||
| - | [[Category: Couture, J | + | [[Category: Couture, J F.]] |
| - | [[Category: Trievel, R | + | [[Category: Trievel, R C.]] |
[[Category: SAH]] | [[Category: SAH]] | ||
[[Category: beta-sheet]] | [[Category: beta-sheet]] | ||
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[[Category: pseudo-knot]] | [[Category: pseudo-knot]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:28 2008'' |
Revision as of 14:16, 21 February 2008
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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 with as ligand. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 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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