3b95: Difference between revisions

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[[Image:3b95.jpg|left|200px]]<br /><applet load="3b95" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:3b95.jpg|left|200px]]
caption="3b95, resolution 2.99&Aring;" />
 
'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)'''<br />
{{Structure
|PDB= 3b95 |SIZE=350|CAPTION= <scene name='initialview01'>3b95</scene>, resolution 2.99&Aring;
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+B+1'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+B+3'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+B+4'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+5'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+A+6'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+A+7'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+A+8'>AC7</scene>, <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+B+9'>AC8</scene> and <scene name='pdbsite=AC9:So4+Binding+Site+For+Residue+A+10'>AC9</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE= EHMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)'''
 
 
==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==
3B95 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences 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]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+B+1'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+B+3'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+B+4'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+5'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+A+6'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Residue+A+7'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Residue+A+8'>AC7</scene>, <scene name='pdbsite=AC8:So4+Binding+Site+For+Residue+B+9'>AC8</scene> and <scene name='pdbsite=AC9:So4+Binding+Site+For+Residue+A+10'>AC9</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B95 OCA].
3B95 is a [[Protein complex]] structure of sequences 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=3B95 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: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 17: Line 32:
[[Category: transferase/structual protein complex]]
[[Category: transferase/structual protein complex]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:04:22 2008''
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Revision as of 19:57, 20 March 2008

File:3b95.jpg


PDB ID 3b95

Drag the structure with the mouse to rotate
, resolution 2.99Å
Sites: , , , , , , , and
Ligands:
Gene: EHMT1 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)


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

3B95 is a Protein complex structure of sequences 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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