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 D Biol Crystallogr. 2014 Sep;70(Pt 9):2401-12. doi: 10.1107/S1399004714014278. Epub 2014 Aug 29.

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.

Keywords: PRMT7; epigenetics; methyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / metabolism*
  • Binding Sites
  • Catalytic Domain
  • Cloning, Molecular
  • Dimerization
  • Methylation
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Sequence Homology, Amino Acid
  • Zinc Fingers*

Substances

  • Arginine
  • PRMT7 protein, mouse
  • Protein-Arginine N-Methyltransferases

Associated data

  • PDB/4C4A