2g46 | pdb_00002g46

structure of vSET in complex with meK27 H3 Pept. and cofactor product SAH

spinqualitylabelsall models 2g46, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2g46 is a 4 chain structure with sequence from Paramecium bursaria chlorella virus 1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SAH NonStd Res: MLZ Gene: A612L (Paramecium bursaria Chlorella virus 1) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone methyltransferase

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