1d2d
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1r1b|1R1B]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d2d OCA], [http://www.ebi.ac.uk/pdbsum/1d2d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d2d RCSB]</span> | ||
}} | }} | ||
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[[Category: trna synthetase (ligase)]] | [[Category: trna synthetase (ligase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:13 2008'' |
Revision as of 16:33, 30 March 2008
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| Related: | 1R1B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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