1d2d
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HAMSTER EPRS SECOND REPEATED ELEMENT; NMR, 15 STRUCTURES
Overview
Aminoacyl-tRNA synthetases of higher eukaryotes possess polypeptide extensions in contrast to their prokaryotic counterparts. These extra domains of poorly understood function are believed to be involved in protein-protein or protein-RNA interactions. Here we showed by gel retardation and filter binding experiments that the repeated units that build the linker region of the bifunctional glutamyl-prolyl-tRNA synthetase had a general RNA-binding capacity. The solution structure of one of these repeated motifs was also solved by NMR spectroscopy. One repeat is built around an antiparallel coiled-coil. Strikingly, the conserved lysine and arginine residues form a basic patch on one side of the structure, presenting a suitable docking surface for nucleic acids. Therefore, this repeated motif may represent a novel type of general RNA-binding domain appended to eukaryotic aminoacyl-tRNA synthetases to serve as a cis-acting tRNA-binding cofactor.
About this Structure
1D2D is a Single protein structure of sequence from Cricetulus griseus. Full crystallographic information is available from OCA.
Reference
A recurrent RNA-binding domain is appended to eukaryotic aminoacyl-tRNA synthetases., Cahuzac B, Berthonneau E, Birlirakis N, Guittet E, Mirande M, EMBO J. 2000 Feb 1;19(3):445-52. PMID:10654942
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