3B3J: The 2.55 A Crystal Structure Of The Apo Catalytic Domain Of Coactivator-Associated Arginine Methyl Transferase I(Carm1:28-507, Residues 28-146 And 479-507 Not Ordered)

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.
PDB ID: 3B3JDownload
MMDB ID: 60724
PDB Deposition Date: 2007/10/22
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.55  Å
Source Organism:
Similar Structures:
Biological Unit for 3B3J: monomeric; determined by author and by software (PISA)
Molecular Components in 3B3J
Label Count Molecule
Protein (1 molecule)
Histone-arginine Methyltransferase Carm1(Gene symbol: Carm1)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB