1ml9: Difference between revisions

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[[Image:1ml9.~~gif~~|left|200px]]

[[Image:1ml9.png|left|200px]]

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~~'''~~Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase~~'''~~

===Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase===

~~==Overview==~~

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~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_12372305}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12372305 is the PubMed ID number.

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==About this Structure==

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[[Category: Adomet-dependent methyltransferase histone h3 lysine-9 methylation]]

[[Category: Dim-5]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ 3 01:22:26 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:15:20 2008''

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-[[Image:1ml9.gif|left|200px]]
+{{Seed}}
+[[Image:1ml9.png|left|200px]]
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 {{STRUCTURE_1ml9|  PDB=1ml9  |  SCENE=  }}
-'''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12372305}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12372305 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12372305}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Adomet-dependent methyltransferase histone h3 lysine-9 methylation]]
 [[Category: Dim-5]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:22:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:15:20 2008''