1zkk
From Proteopedia
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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 SAH 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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