2OQB

Crystal structure of the N-terminal domain of coactivator-associated methyltransferase 1 (CARM1)

Summary for 2OQB

• Entry DOI: 10.2210/pdb2oqb/pdb
• Descriptor: Histone-arginine methyltransferase CARM1, CHLORIDE ION (3 entities in total)
• Functional Keywords: protein arginine methyltransferase, transcriptional regulation, activation domain, transferase, gene regulation
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Nucleus: Q4AE70
• Total number of polymer chains: 2
• Total formula weight: 25732.57

Authors

Cavarelli, J. (deposition date: 2007-01-31, release date: 2007-10-30, Last modification date: 2023-12-27)

Primary citation

Troffer-Charlier, N.,Cura, V.,Hassenboehler, P.,Moras, D.,Cavarelli, J.
Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains.
Embo J., 26:4391-4401, 2007

PubMed Abstract: 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.

PubMed: 17882262
DOI: 10.1038/sj.emboj.7601855

Experimental method

X-RAY DIFFRACTION (1.69 Å)