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.

Date publication

septembre 2014

Auteurs

Membres identifiés du Cancéropôle Est :
Pr CAVARELLI Jean

Tous les auteurs :
Cura V, Troffer-Charlier N, Wurtz JM, Bonnefond L, Cavarelli J

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/25195753

Résumé

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 A 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.

Référence

Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2401-12