4c4a is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.
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.,Cura V, Troffer-Charlier N, Wurtz JM, Bonnefond L, Cavarelli J Acta Crystallogr D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2401-12. doi:, 10.1107/S1399004714014278. Epub 2014 Aug 29. PMID:25195753[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Cura V, Troffer-Charlier N, Wurtz JM, 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 D Biol Crystallogr. 2014 Sep 1;70(Pt 9):2401-12. doi:, 10.1107/S1399004714014278. Epub 2014 Aug 29. PMID:25195753 doi:http://dx.doi.org/10.1107/S1399004714014278
