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1ml9

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[[Image:1ml9.gif|left|200px]]<br /><applet load="1ml9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ml9.gif|left|200px]]
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caption="1ml9, resolution 1.98&Aring;" />
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'''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase'''<br />
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{{Structure
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|PDB= 1ml9 |SIZE=350|CAPTION= <scene name='initialview01'>1ml9</scene>, resolution 1.98&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Structure of the Neurospora SET domain protein DIM-5, a histone lysine methyltransferase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1ML9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ML9 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12372305 12372305]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12372305 12372305]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Neurospora crassa]]
[[Category: Neurospora crassa]]
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[[Category: dim-5]]
[[Category: dim-5]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:44:53 2008''

Revision as of 10:44, 20 March 2008


PDB ID 1ml9

Drag the structure with the mouse to rotate
, resolution 1.98Å
Ligands: and
Activity: Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Coordinates: save as pdb, mmCIF, xml



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. 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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