Structure of the S. pombe Clr4 catalytic domain bound to SAMStructure of the S. pombe Clr4 catalytic domain bound to SAM

Structural highlights

6bp4 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CLR4_SCHPO] Histone methyltransferase. Catalytic component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.[1] [2]

References

  1. Horn PJ, Bastie JN, Peterson CL. A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation. Genes Dev. 2005 Jul 15;19(14):1705-14. PMID:16024659 doi:http://dx.doi.org/10.1101/gad.1328005
  2. Ekwall K, Ruusala T. Mutations in rik1, clr2, clr3 and clr4 genes asymmetrically derepress the silent mating-type loci in fission yeast. Genetics. 1994 Jan;136(1):53-64. PMID:8138176

6bp4, resolution 2.77Å

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