2f69
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(New page: 200px<br /> <applet load="2f69" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f69, resolution 1.30Å" /> '''Ternary complex of ...)
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Revision as of 19:53, 12 November 2007
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Ternary complex of SET7/9 bound to AdoHcy and a TAF10 peptide
Overview
Human SET7/9 is a protein lysine methyltransferase (PKMT) that methylates, histone H3, the tumor suppressor p53 and the TBP-associated factor TAF10., To elucidate the determinants of its substrate specificity, we have solved, the enzyme's structure bound to a TAF10 peptide and examined its ability, to methylate histone H3, TAF10 and p53 substrates bearing either mutations, or covalent modifications within their respective methylation sites., Collectively, our data reveal that SET7/9 recognizes a conserved K/R-S/T/A, motif preceding the lysine substrate and has a propensity to bind, aspartates and asparagines on the C-terminal side of the lysine target. We, then used a sequence-based approach with this motif to identify novel, substrates for this PKMT. Among the putative targets is TAF7, which is, methylated at Lys5 by the enzyme in vitro. These results demonstrate the, predictive value of the consensus motif in identifying novel substrates, for SET7/9.
About this Structure
2F69 is a Single protein structure of sequence from Homo sapiens with ACE and SAH as ligands. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
Structural basis for the methylation site specificity of SET7/9., Couture JF, Collazo E, Hauk G, Trievel RC, Nat Struct Mol Biol. 2006 Feb;13(2):140-6. Epub 2006 Jan 15. PMID:16415881
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