1MVH

structure of the SET domain histone lysine methyltransferase Clr4

Summary for 1MVH

• Entry DOI: 10.2210/pdb1mvh/pdb
• Descriptor: Cryptic loci regulator 4, SULFATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: lysine methyltransferase, clr4, set-domain, transferase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Cellular location: Nucleus: O60016
• Total number of polymer chains: 1
• Total formula weight: 34274.88

Authors

Min, J.R.,Zhang, X.,Cheng, X.D.,Grewal, S.I.S.,Xu, R.-M. (deposition date: 2002-09-25, release date: 2002-10-30, Last modification date: 2024-02-14)

Primary citation

Min, J.,Zhang, X.,Cheng, X.,Grewal, S.I.,Xu, R.M.
Structure of the SET domain histone lysine methyltransferase Clr4.
Nat.Struct.Biol., 9:828-832, 2002

PubMed Abstract: Methylation of histone H3 lysine 9 is an important component of the 'histone code' for heterochromatic gene silencing. The SET domain-containing Clr4 protein, a close relative of Su(var)3-9 proteins in higher eukaryotes, specifically methylates lysine 9 of histone H3 and is essential for silencing in Schizosaccharomyces pombe. Here we report the 2.3 A resolution crystal structure of the catalytic domain of Clr4. The structure reveals an overall fold rich in beta-strands, a potential active site consisting of a SAM-binding pocket, and a connected groove that could accommodate the binding of the N-terminal tail of histone H3. The pre-SET motif contains a triangular zinc cluster coordinated by nine cysteines distant from the active site, whereas the post-SET region is largely flexible but proximal to the active site. The structure provides insights into the architecture of SET domain histone methyltransferases and establishes a paradigm for further characterization of the Clr4 family of epigenetic regulators.

PubMed: 12389037

Experimental method

X-RAY DIFFRACTION (2.3 Å)