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1r1b

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1b OCA], [http://www.ebi.ac.uk/pdbsum/1r1b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r1b RCSB]</span>
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[[Category: trna synthetase (ligase)]]
[[Category: trna synthetase (ligase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:54 2008''

Revision as of 20:21, 30 March 2008


PDB ID 1r1b

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE


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

1R1B 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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