3b7b: Difference between revisions

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[[Image:3b7b.jpg|left|200px]]<br /><applet load="3b7b" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:3b7b.jpg|left|200px]]
caption="3b7b, resolution 2.99&Aring;" />
 
'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)'''<br />
{{Structure
|PDB= 3b7b |SIZE=350|CAPTION= <scene name='initialview01'>3b7b</scene>, resolution 2.99&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+5'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+6'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+7'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+8'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+1'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+B+2'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+B+3'>AC7</scene> and <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+B+4'>AC8</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|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]
|GENE= EHMT1, EUHMTASE1, KIAA1876 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)'''
 
 
==Overview==
Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.


==About this Structure==
==About this Structure==
3B7B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+5'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+6'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+7'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+8'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+1'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+B+2'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+B+3'>AC7</scene> and <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+B+4'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7B OCA].
3B7B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7B OCA].  
 
==Reference==
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules., Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X, Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18264113 18264113]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Histone-lysine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 23: Line 38:
[[Category: transferase]]
[[Category: transferase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:49 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:56:46 2008''

Revision as of 19:56, 20 March 2008

File:3b7b.jpg


PDB ID 3b7b

Drag the structure with the mouse to rotate
, resolution 2.99Å
Sites: , , , , , , and
Ligands:
Gene: EHMT1, EUHMTASE1, KIAA1876 (Homo sapiens)
Activity: Histone-lysine N-methyltransferase, with EC number 2.1.1.43
Coordinates: save as pdb, mmCIF, xml



EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)


OverviewOverview

Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.

About this StructureAbout this Structure

3B7B is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules., Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X, Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10. PMID:18264113

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