3b95
From Proteopedia
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|PDB= 3b95 |SIZE=350|CAPTION= <scene name='initialview01'>3b95</scene>, resolution 2.99Å | |PDB= 3b95 |SIZE=350|CAPTION= <scene name='initialview01'>3b95</scene>, resolution 2.99Å | ||
|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> | |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> | + | |LIGAND= <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= EHMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= EHMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3b7b|3B7B]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b95 OCA], [http://www.ebi.ac.uk/pdbsum/3b95 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b95 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
| + | |||
| + | ==Disease== | ||
| + | Known disease associated with this structure: Chromosome 9q subtelomeric deletion syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607001 607001]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Collins, R E.]] | [[Category: Collins, R E.]] | ||
[[Category: Horton, J R.]] | [[Category: Horton, J R.]] | ||
| - | [[Category: SO4]] | ||
[[Category: ank repeat]] | [[Category: ank repeat]] | ||
[[Category: ankyrin repeat]] | [[Category: ankyrin repeat]] | ||
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[[Category: transferase/structual protein complex]] | [[Category: transferase/structual protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:24:19 2008'' |
Revision as of 02:24, 31 March 2008
| |||||||
| , resolution 2.99Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | EHMT1 (Homo sapiens) | ||||||
| Related: | 3B7B
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)
Contents |
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.
Disease
Known disease associated with this structure: Chromosome 9q subtelomeric deletion syndrome OMIM:[607001]
About this Structure
3B95 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from 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:18264113
Page seeded by OCA on Mon Mar 31 05:24:19 2008
