1n3j

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(New page: 200px<br /><applet load="1n3j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n3j" /> '''Structure and Substrate of a Histone H3 Lysi...)
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'''Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1'''<br />
'''Structure and Substrate of a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1N3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N3J OCA].
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1N3J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_bursaria_chlorella_virus_1 Paramecium bursaria chlorella virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3J OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Farooq, A.]]
[[Category: Farooq, A.]]
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[[Category: Koch, A.W.]]
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[[Category: Koch, A W.]]
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[[Category: Manzur, K.L.]]
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[[Category: Manzur, K L.]]
[[Category: Plotnikova, O.]]
[[Category: Plotnikova, O.]]
[[Category: Sachchidanand]]
[[Category: Sachchidanand]]
[[Category: Zeng, L.]]
[[Category: Zeng, L.]]
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[[Category: Zhou, M.M.]]
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[[Category: Zhou, M M.]]
[[Category: beta barrel]]
[[Category: beta barrel]]
[[Category: homodimer]]
[[Category: homodimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:30:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:49 2008''

Revision as of 12:01, 21 February 2008


1n3j

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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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