1ml9 | pdb_00001ml9

Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase

spinqualitylabelsall models 1ml9, resolution 1.98Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ml9 is a 1 chain structure with sequence from Chrysonilia crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: UNK, ZN Activity: Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Resources: FirstGlance, OCA, PDBe, 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 AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase.,Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X Cell. 2002 Oct 4;111(1):117-27. PMID:12372305 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone methyltransferase

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