1R1B: EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE

Citation:
Abstract
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.
PDB ID: 1R1BDownload
MMDB ID: 11802
PDB Deposition Date: 1998/12/15
Updated in MMDB: 2007/10
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1R1B
Label Count Molecule
Protein (1 molecule)
1
tRNA Synthetase
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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