2oqb
From Proteopedia
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|PDB= 2oqb |SIZE=350|CAPTION= <scene name='initialview01'>2oqb</scene>, resolution 1.690Å | |PDB= 2oqb |SIZE=350|CAPTION= <scene name='initialview01'>2oqb</scene>, resolution 1.690Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-arginine_N-methyltransferase Histone-arginine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.125 2.1.1.125] </span> |
|GENE= Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqb OCA], [http://www.ebi.ac.uk/pdbsum/2oqb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oqb RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cavarelli, J.]] | [[Category: Cavarelli, J.]] | ||
| - | [[Category: CL]] | ||
[[Category: activation domain]] | [[Category: activation domain]] | ||
| - | [[Category: gene regulation]] | ||
[[Category: protein arginine methyltransferase]] | [[Category: protein arginine methyltransferase]] | ||
[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | [[Category: transferase]] | + | [[Category: transferase,gene regulation]] |
| - | ''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 04:21:37 2008'' |
Revision as of 01:21, 31 March 2008
| |||||||
| , resolution 1.690Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Carm1, Prmt4 (Rattus norvegicus) | ||||||
| Activity: | Histone-arginine N-methyltransferase, with EC number 2.1.1.125 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)
Overview
Coactivator-associated arginine methyltransferase 1 (CARM1), a protein arginine methyltransferase recruited by several transcription factors, methylates a large variety of proteins and plays a critical role in gene expression. We report, in this paper, four crystal structures of isolated modules of CARM1. The 1.7 A crystal structure of the N-terminal domain of CARM1 reveals an unexpected PH domain, a scaffold frequently found to regulate protein-protein interactions in a large variety of biological processes. Three crystal structures of the CARM1 catalytic module, two free and one cofactor-bound forms (refined at 2.55 A, 2.4 A and 2.2 A, respectively) reveal large structural modifications including disorder to order transition, helix to strand transition and active site modifications. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may inspire how CARM1 regulates its biological activities by protein-protein interactions.
About this Structure
2OQB is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains., Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J, EMBO J. 2007 Oct 17;26(20):4391-401. Epub 2007 Sep 20. PMID:17882262
Page seeded by OCA on Mon Mar 31 04:21:37 2008
