1mt6: Difference between revisions

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==Overview==
==Overview==
The SET domain contains the catalytic center of lysine methyltransferases, that target the N-terminal tails of histones and regulate chromatin, function. Here we report the structure of the SET7/9 protein in the, absence and presence of its cofactor product, S-adenosyl-L-homocysteine, (AdoHcy). A knot within the SET domain helps form the methyltransferase, active site, where AdoHcy binds and lysine methylation is likely to occur., A structure-guided comparison of sequences within the SET protein family, suggests that the knot substructure and active site environment are, conserved features of the SET domain.
The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.


==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Devarakonda, S.]]
[[Category: Devarakonda, S.]]
[[Category: Harp, J.M.]]
[[Category: Harp, J M.]]
[[Category: Jacobs, S.A.]]
[[Category: Jacobs, S A.]]
[[Category: Khorasanizadeh, S.]]
[[Category: Khorasanizadeh, S.]]
[[Category: Kim, Y.]]
[[Category: Kim, Y.]]
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[[Category: set domain]]
[[Category: set domain]]


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Revision as of 14:58, 21 February 2008

File:1mt6.jpg


1mt6, resolution 2.20Å

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Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy

OverviewOverview

The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.

About this StructureAbout this Structure

1MT6 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.

ReferenceReference

The active site of the SET domain is constructed on a knot., Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S, Nat Struct Biol. 2002 Nov;9(11):833-8. PMID:12389038

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