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| | ==Crystal structure of Arginyl-tRNA synthetase== | | ==Crystal structure of Arginyl-tRNA synthetase== |
| - | <StructureSection load='4q2y' size='340' side='right' caption='[[4q2y]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4q2y' size='340' side='right'caption='[[4q2y]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q2y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q2t|4q2t]], [[4q2x|4q2x]]</td></tr> | + | </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=4q2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2y OCA], [https://pdbe.org/4q2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2y RCSB], [https://www.ebi.ac.uk/pdbsum/4q2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2y ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RARS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2y OCA], [http://pdbe.org/4q2y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q2y RCSB], [http://www.ebi.ac.uk/pdbsum/4q2y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYRC_HUMAN SYRC_HUMAN]] Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.<ref>PMID:17443684</ref> | + | [https://www.uniprot.org/uniprot/SYRC_HUMAN SYRC_HUMAN] Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.<ref>PMID:17443684</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4q2y" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4q2y" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arginine--tRNA ligase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Cha, S Y]] | + | [[Category: Cha SY]] |
| - | [[Category: Han, A R]] | + | [[Category: Han AR]] |
| - | [[Category: Hwang, K Y]] | + | [[Category: Hwang KY]] |
| - | [[Category: Jo, C H]] | + | [[Category: Jo CH]] |
| - | [[Category: Kim, H S]] | + | [[Category: Kim HS]] |
| - | [[Category: Arginine binding]]
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| - | [[Category: Arginine-trna ligase]]
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| - | [[Category: Atp binding]]
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| - | [[Category: High region]]
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| - | [[Category: Ligase]]
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| - | [[Category: Trna binding]]
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| Structural highlights
Function
SYRC_HUMAN Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.[1]
Publication Abstract from PubMed
Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of l-arginine to its cognate tRNA. l-Canavanine, a structural analog of l-arginine, has recently been studied as an anticancer agent. Here, we determined the crystal structures of the apo, l-arginine-complexed, and l-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). Similar interactions were formed upon binding to l-canavanine or l-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. Detailed conformational changes that occur upon substrate binding were explained. The hArgRS structure was also compared with previously reported homologue structures. The results presented here may provide a basis for the design of new anticancer drugs, such as l-canavanine analogs.
The crystal structure of arginyl-tRNA synthetase from Homo sapiens.,Kim HS, Cha SY, Jo CH, Han A, Hwang KY FEBS Lett. 2014 Jun 27;588(14):2328-34. doi: 10.1016/j.febslet.2014.05.027. Epub , 2014 May 22. PMID:24859084[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli MC, Uberti EC. Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. J Cell Physiol. 2007 Aug;212(2):293-7. PMID:17443684 doi:http://dx.doi.org/10.1002/jcp.21083
- ↑ Kim HS, Cha SY, Jo CH, Han A, Hwang KY. The crystal structure of arginyl-tRNA synthetase from Homo sapiens. FEBS Lett. 2014 Jun 27;588(14):2328-34. doi: 10.1016/j.febslet.2014.05.027. Epub , 2014 May 22. PMID:24859084 doi:http://dx.doi.org/10.1016/j.febslet.2014.05.027
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