This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3b7b
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:3b7b.jpg|left|200px]] | + | [[Image:3b7b.jpg|left|200px]] |
| - | + | ||
| - | '''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)''' | + | {{Structure |
| + | |PDB= 3b7b |SIZE=350|CAPTION= <scene name='initialview01'>3b7b</scene>, resolution 2.99Å | ||
| + | |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 [ | + | 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 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:56:46 2008'' |
Revision as of 16:56, 20 March 2008
| |||||||
| , 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)
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
3B7B is a Single protein structure of sequence 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 Thu Mar 20 18:56:46 2008
Categories: Histone-lysine N-methyltransferase | Homo sapiens | Single protein | Cheng, X. | Collins, R E. | Horton, J R. | SO4 | Alternative splicing | Ank repeat | Ankyrin repeat | Chromatin regulator | Methyltransferase | Nucleus | Phosphorylation | Polymorphism | S-adenosyl-l-methionine | Transferase
