4C4A

Crystal structure of mouse protein arginine methyltransferase 7 in complex with SAH

Summary for 4C4A

• Entry DOI: 10.2210/pdb4c4a/pdb
• Descriptor: PROTEIN ARGININE N-METHYLTRANSFERASE 7, S-ADENOSYL-L-HOMOCYSTEINE, 3-[BENZYL(DIMETHYL)AMMONIO]PROPANE-1-SULFONATE, ... (6 entities in total)
• Functional Keywords: transferase
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Cytoplasm, cytosol : Q922X9
• Total number of polymer chains: 1
• Total formula weight: 79218.40

Authors

Cura, V.,Troffer-Charlier, N.,Bonnefond, L.,Wurtz, J.M.,Cavarelli, J. (deposition date: 2013-09-02, release date: 2014-07-02, Last modification date: 2024-05-01)

Primary citation

Cura, V.,Troffer-Charlier, N.,Wurtz, J.M.,Bonnefond, L.,Cavarelli, J.
Structural Insight Into Arginine Methylation by the Mouse Protein Arginine Methyltransferase 7: A Zinc Finger Freezes the Mimic of the Dimeric State Into a Single Active Site.
Acta Crystallogr.,Sect.D, 70:2401-, 2014

PubMed Abstract: Protein arginine methyltransferase 7 (PRMT7) is a type III arginine methyltransferase which has been implicated in several biological processes such as transcriptional regulation, DNA damage repair, RNA splicing, cell differentiation and metastasis. PRMT7 is a unique but less characterized member of the family of PRMTs. The crystal structure of full-length PRMT7 from Mus musculus refined at 1.7 Å resolution is described. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The high-resolution crystal structure presented here revealed several structural features showing that the second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops.

PubMed: 25195753
DOI: 10.1107/S1399004714014278

Experimental method

X-RAY DIFFRACTION (1.7 Å)