5zdo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure Analysis of TtQRS in co-crystallised with ATP== | |
| + | <StructureSection load='5zdo' size='340' side='right' caption='[[5zdo]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zdo]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZDO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--tRNA_ligase Glutamine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.18 6.1.1.18] </span></td></tr> | ||
| + | <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=5zdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zdo OCA], [http://pdbe.org/5zdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zdo RCSB], [http://www.ebi.ac.uk/pdbsum/5zdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zdo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aminoacyl-tRNA synthetases (AaRSs) are vital enzymes for translation of proteins in cells. AaRSs catalyse the esterification of a specific amino acid to corresponding tRNAs to form an aminoacyl-tRNA that is used in ribosome-based protein synthesis. We focused on Glutaminyl tRNA synthetase (GlnRS) enzyme from the extreme thermophile Thermus thermophilus for structural studies. Our thermal shift assays show binding of enzyme substrates L-Gln and ATP as well as of various metals including cesium. We resolved crystal structures of apo-GlnRS as well as those in complex with AMP and ATP at 2.8A, 2.4A and 2.6A respectively. The bound cesium was found at the site of magnesium that typically binds to GlnRS. High structural conservation was evident in the Thermus thermophilus GlnRS when compared to those from Escherichia coli GlnRS. | ||
| - | + | Structural and functional analysis of Glutaminyl-tRNA synthetase (TtGlnRS) from Thermus thermophilus HB8 and its complexes.,Nachiappan M, Jain V, Sharma A, Yogavel M, Jeyakanthan J Int J Biol Macromol. 2018 Dec;120(Pt B):1379-1386. doi:, 10.1016/j.ijbiomac.2018.09.115. Epub 2018 Sep 21. PMID:30248426<ref>PMID:30248426</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5zdo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Glutamine--tRNA ligase]] | ||
[[Category: Jain, V]] | [[Category: Jain, V]] | ||
| - | [[Category: Manickam, Y]] | ||
[[Category: Jeyaraman, J]] | [[Category: Jeyaraman, J]] | ||
| + | [[Category: Manickam, Y]] | ||
[[Category: Mutharasappan, N]] | [[Category: Mutharasappan, N]] | ||
[[Category: Sharma, A]] | [[Category: Sharma, A]] | ||
| + | [[Category: Glnr]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Qr]] | ||
| + | [[Category: Synthetase]] | ||
Revision as of 06:30, 5 December 2018
Crystal Structure Analysis of TtQRS in co-crystallised with ATP
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Categories: Glutamine--tRNA ligase | Jain, V | Jeyaraman, J | Manickam, Y | Mutharasappan, N | Sharma, A | Glnr | Ligase | Qr | Synthetase
