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

Structural highlights

1ml9 is a 1 chain structure with sequence from Neurospora crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DIM5_NEUCR Histone methyltransferase that specifically trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA methylation.[1] [2] [3] [4]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Tamaru H, Selker EU. A histone H3 methyltransferase controls DNA methylation in Neurospora crassa. Nature. 2001 Nov 15;414(6861):277-83. PMID:11713521 doi:http://dx.doi.org/10.1038/35104508
  2. Tamaru H, Zhang X, McMillen D, Singh PB, Nakayama J, Grewal SI, Allis CD, Cheng X, Selker EU. Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in Neurospora crassa. Nat Genet. 2003 May;34(1):75-9. PMID:12679815 doi:http://dx.doi.org/10.1038/ng1143
  3. Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X. Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase. Cell. 2002 Oct 4;111(1):117-27. PMID:12372305
  4. Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X. Structural basis for the product specificity of histone lysine methyltransferases. Mol Cell. 2003 Jul;12(1):177-85. PMID:12887903

1ml9, resolution 1.98Å

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