1r1b
From Proteopedia
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| - | [[Image:1r1b.jpg|left|200px]] | ||
| - | < | + | ==EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE== |
| - | + | <StructureSection load='1r1b' size='340' side='right'caption='[[1r1b]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1r1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetulus_griseus Cricetulus griseus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1B FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | --> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1b OCA], [https://pdbe.org/1r1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1b RCSB], [https://www.ebi.ac.uk/pdbsum/1r1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1b ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/SYEP_CRIGR SYEP_CRIGR] | |
| - | + | == Evolutionary Conservation == | |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | == | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/1r1b_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r1b ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:10654942</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | <div class="pdbe-citations 1r1b" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Cricetulus griseus]] | [[Category: Cricetulus griseus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Berthonneau | + | [[Category: Berthonneau E]] |
| - | [[Category: Birlirakis | + | [[Category: Birlirakis N]] |
| - | [[Category: Cahuzac | + | [[Category: Cahuzac B]] |
| - | [[Category: Guittet | + | [[Category: Guittet E]] |
| - | [[Category: Mirande | + | [[Category: Mirande M]] |
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Current revision
EPRS SECOND REPEATED ELEMENT, NMR, MINIMIZED AVERAGE STRUCTURE
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