1n3j
From Proteopedia
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Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1
Overview
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.
About this Structure
1N3J is a Single protein structure of sequence from Paramecium bursaria chlorella virus 1. Full crystallographic information is available from OCA.
Reference
A dimeric viral SET domain methyltransferase specific to Lys27 of histone H3., Manzur KL, Farooq A, Zeng L, Plotnikova O, Koch AW, Sachchidanand, Zhou MM, Nat Struct Biol. 2003 Mar;10(3):187-96. PMID:12567185
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