1ml9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ml9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ml9, resolution 1.98&Aring;" /> '''Structure of the Neu...)
Line 1: Line 1:
-
[[Image:1ml9.gif|left|200px]]<br /><applet load="1ml9" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ml9.gif|left|200px]]<br /><applet load="1ml9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ml9, resolution 1.98&Aring;" />
caption="1ml9, resolution 1.98&Aring;" />
'''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", 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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ML9 OCA].
+
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.R.]]
+
[[Category: Horton, J R.]]
-
[[Category: Keefe, L.J.]]
+
[[Category: Keefe, L J.]]
-
[[Category: Khan, S.I.]]
+
[[Category: Khan, S I.]]
-
[[Category: Selker, E.U.]]
+
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:30:00 2007''
+
''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


1ml9, resolution 1.98Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:56:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools