2g46
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(New page: 200px<br /><applet load="2g46" size="350" color="white" frame="true" align="right" spinBox="true" caption="2g46" /> '''structure of vSET in complex with meK27 H3 P...)
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Revision as of 17:51, 29 January 2008
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structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH
Overview
SET domain lysine methyltransferases are known to catalyze site and, state-specific methylation of lysine residues in histones that is, fundamental in epigenetic regulation of gene activation and silencing in, eukaryotic organisms. Here we report the three-dimensional solution, structure of the SET domain histone lysine methyltransferase (vSET) from, Paramecium bursaria chlorella virus 1 bound to cofactor, S-adenosyl-L-homocysteine and a histone H3 peptide containing, mono-methylated lysine 27. The dimeric structure, mimicking an, enzyme/cofactor/substrate complex, yields the structural basis of the, substrate specificity and methylation multiplicity of the enzyme. Our, results from mutagenesis and enzyme kinetics analyses argue that a general, base mechanism is less likely for lysine methylation by SET domains; and, that the only invariant active site residue tyrosine 105 in vSET, facilitates methyl transfer from cofactor to the substrate lysine by, aligning intermolecular interactions in the lysine access channel of the, enzyme.
About this Structure
2G46 is a Single protein structure of sequence from Paramecium bursaria chlorella virus 1 with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insights of the specificity and catalysis of a viral histone H3 lysine 27 methyltransferase., Qian C, Wang X, Manzur K, Sachchidanand, Farooq A, Zeng L, Wang R, Zhou MM, J Mol Biol. 2006 May 26;359(1):86-96. Epub 2006 Mar 20. PMID:16603186
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