Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold
2hqt is a 20 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
ARC1_YEAST Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.[1][2][3][4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Deinert K, Fasiolo F, Hurt EC, Simos G. Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J Biol Chem. 2001 Feb 23;276(8):6000-8. PMID:11069915 doi:10.1074/jbc.M008682200
↑Golinelli-Cohen MP, Mirande M. Arc1p is required for cytoplasmic confinement of synthetases and tRNA. Mol Cell Biochem. 2007 Jun;300(1-2):47-59. PMID:17131041 doi:10.1007/s11010-006-9367-4
↑Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the EMBO J. 1996 Oct 1;15(19):5437-48 PMID:8895587
↑Simos G, Sauer A, Fasiolo F, Hurt EC. A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases. Mol Cell. 1998 Jan;1(2):235-42. PMID:9659920 doi:10.1016/s1097-2765(00)80024-6
