1ml9: Difference between revisions
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'''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase''' | '''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase''' | ||
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[[Category: Tamaru, H.]] | [[Category: Tamaru, H.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
[[Category: | [[Category: Adomet-dependent methyltransferase histone h3 lysine-9 methylation]] | ||
[[Category: | [[Category: Dim-5]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:22:26 2008'' | |||
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Revision as of 01:22, 3 May 2008
Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase
OverviewOverview
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.
About this StructureAbout this Structure
1ML9 is a Single protein structure of sequence from Neurospora crassa. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 01:22:26 2008