1n3j
From Proteopedia
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'''Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1''' | '''Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1''' | ||
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[[Category: Zeng, L.]] | [[Category: Zeng, L.]] | ||
[[Category: Zhou, M M.]] | [[Category: Zhou, M M.]] | ||
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| - | [[Category: | + | [[Category: Homodimer]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:02:44 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:02, 2 May 2008
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 Page seeded by OCA on Sat May 3 02:02:44 2008
