title: 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.
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.
authors.affiliation: Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.
authors.forename: Vincent
authors.initials: V
authors.lastname: Cura
authors.affiliation: Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.
authors.forename: Nathalie
authors.initials: N
authors.lastname: Troffer-Charlier
authors.affiliation: Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.
authors.forename: Jean Marie
authors.initials: JM
authors.lastname: Wurtz
authors.affiliation: Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.
authors.forename: Luc
authors.initials: L
authors.lastname: Bonnefond
authors.affiliation: Département de Biologie Structurale Intégrative, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg, CNRS UMR7104, INSERM U596, 1 Rue Laurent Fries, F-67404 Illkirch, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Cavarelli
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D001665:Binding Sites; D020134:Catalytic Domain; D003001:Cloning, Molecular; D019281:Dimerization; D008745:Methylation; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011484:Protein-Arginine N-Methyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D016335:Zinc Fingers
chemical_list: D001120:Arginine; C570798:PRMT7 protein, mouse; D011484:Protein-Arginine N-Methyltransferases
keywords: PRMT7; epigenetics; methyltransferase