1N3J
Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1
Summary for 1N3J
| Entry DOI | 10.2210/pdb1n3j/pdb |
| NMR Information | BMRB: 5567 |
| Descriptor | Histone H3 Lysine Methyltransferase (1 entity in total) |
| Functional Keywords | beta barrel, homodimer, transferase |
| Biological source | Paramecium bursaria Chlorella virus 1 |
| Total number of polymer chains | 2 |
| Total formula weight | 27213.25 |
| Authors | Manzur, K.L.,Farooq, A.,Zeng, L.,Plotnikova, O.,Sachchidanand,Koch, A.W.,Zhou, M.-M. (deposition date: 2002-10-28, release date: 2003-01-28, Last modification date: 2024-05-22) |
| Primary citation | Manzur, K.L.,Farooq, A.,Zeng, L.,Plotnikova, O.,Koch, A.W.,Sachchidanand,Zhou, M.-M. A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3. Nat.Struct.Biol., 10:187-196, 2003 Cited by PubMed Abstract: Site-specific lysine methylation of histones by SET domains is a hallmark for epigenetic control of gene transcription in eukaryotic organisms. Here we report that a SET domain protein from Paramecium bursaria chlorella virus can specifically di-methylate Lys27 in histone H3, a modification implicated in gene silencing. The solution structure of the viral SET domain reveals a butterfly-shaped head-to-head symmetric dimer different from other known protein methyltransferases. Each subunit consists of a Greek-key antiparallel beta-barrel and a three-stranded open-faced sandwich that mediates the dimer interface. Cofactor S-adenosyl-L-methionine (SAM) binds at the opening of the beta-barrel, and amino acids C-terminal to Lys27 in H3 and in the flexible C-terminal tail of the enzyme confer the specificity of this viral histone methyltransferase. PubMed: 12567185DOI: 10.1038/nsb898 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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