1muf
From Proteopedia
(New page: 200px<br /> <applet load="1muf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1muf, resolution 2.26Å" /> '''Structure of histon...) |
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| - | [[Image:1muf.gif|left|200px]]<br /> | + | [[Image:1muf.gif|left|200px]]<br /><applet load="1muf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1muf" size=" | + | |
caption="1muf, resolution 2.26Å" /> | caption="1muf, resolution 2.26Å" /> | ||
'''Structure of histone H3 K4-specific methyltransferase SET7/9'''<br /> | '''Structure of histone H3 K4-specific methyltransferase SET7/9'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The SET domain contains the catalytic center of lysine methyltransferases | + | 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== | ||
| - | 1MUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http:// | + | 1MUF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Devarakonda, S.]] | [[Category: Devarakonda, S.]] | ||
| - | [[Category: Harp, J | + | [[Category: Harp, J M.]] |
| - | [[Category: Jacobs, S | + | [[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]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:05 2008'' |
Revision as of 11:59, 21 February 2008
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Structure of histone H3 K4-specific methyltransferase SET7/9
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.
About this Structure
1MUF is a Single protein structure of sequence from Homo sapiens. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
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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