1r1b
From Proteopedia
(New page: 200px<br /><applet load="1r1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1b" /> '''EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED...) |
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| - | [[Image:1r1b.jpg|left|200px]]<br /><applet load="1r1b" size=" | + | [[Image:1r1b.jpg|left|200px]]<br /><applet load="1r1b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r1b" /> | caption="1r1b" /> | ||
'''EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | '''EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aminoacyl-tRNA synthetases of higher eukaryotes possess polypeptide | + | 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== | ==About this Structure== | ||
| - | 1R1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http:// | + | 1R1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trna synthetase (ligase)]] | [[Category: trna synthetase (ligase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:58 2008'' |
Revision as of 12:45, 21 February 2008
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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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