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1ml9
From Proteopedia
(New page: 200px<br /><applet load="1ml9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ml9, resolution 1.98Å" /> '''Structure of the Neu...) |
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| - | [[Image:1ml9.gif|left|200px]]<br /><applet load="1ml9" size=" | + | [[Image:1ml9.gif|left|200px]]<br /><applet load="1ml9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ml9, resolution 1.98Å" /> | caption="1ml9, resolution 1.98Å" /> | ||
'''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase'''<br /> | '''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | AdoMet-dependent methylation of histones is part of the "histone code" | + | AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain. |
==About this Structure== | ==About this Structure== | ||
| - | 1ML9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] with ZN and UNK as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1ML9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=UNK:'>UNK</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1ML9 OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
| - | [[Category: Horton, J | + | [[Category: Horton, J R.]] |
| - | [[Category: Keefe, L | + | [[Category: Keefe, L J.]] |
| - | [[Category: Khan, S | + | [[Category: Khan, S I.]] |
| - | [[Category: Selker, E | + | [[Category: Selker, E U.]] |
[[Category: Tamaru, H.]] | [[Category: Tamaru, H.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
| Line 26: | Line 26: | ||
[[Category: dim-5]] | [[Category: dim-5]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:22 2008'' |
Revision as of 11:56, 21 February 2008
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Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase
Overview
AdoMet-dependent methylation of histones is part of the "histone code" that can profoundly influence gene expression. We describe the crystal structure of Neurospora DIM-5, a histone H3 lysine 9 methyltranferase (HKMT), determined at 1.98 A resolution, as well as results of biochemical characterization and site-directed mutagenesis of key residues. This SET domain protein bears no structural similarity to previously characterized AdoMet-dependent methyltransferases but includes notable features such as a triangular Zn3Cys9 zinc cluster in the pre-SET domain and a AdoMet binding site in the SET domain essential for methyl transfer. The structure suggests a mechanism for the methylation reaction and provides the structural basis for functional characterization of the HKMT family and the SET domain.
About this Structure
1ML9 is a Single protein structure of sequence from Neurospora crassa with and as ligands. Active as Histone-lysine N-methyltransferase, with EC number 2.1.1.43 Full crystallographic information is available from OCA.
Reference
Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase., Zhang X, Tamaru H, Khan SI, Horton JR, Keefe LJ, Selker EU, Cheng X, Cell. 2002 Oct 4;111(1):117-27. PMID:12372305
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