4oby
From Proteopedia
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| - | + | ==Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition== | |
| - | + | <StructureSection load='4oby' size='340' side='right' caption='[[4oby]], [[Resolution|resolution]] 2.57Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4oby]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OBY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">argS, b1876, JW1865 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
| + | <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> | ||
| + | <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=4oby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oby OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oby RCSB], [http://www.ebi.ac.uk/pdbsum/4oby PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The arginyl-tRNA synthetase (ArgRS) catalyzes the esterification reaction between L-arginine and its cognate tRNAArg. Previously reported structures of ArgRS shed considerable light on the tRNA recognition mechanism, while the aspect of amino acid binding in ArgRS remains largely unexplored. Here we report the first crystal structure of E. coli ArgRS (eArgRS) complexed with L-arginine, and a series of mutational studies using isothermal titration calorimetry (ITC). Combined with previously reported work on ArgRS, our results elucidated the structural and functional roles of a series of important residues in the active site, which furthered our understanding of this unique enzyme. | ||
| - | + | Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition.,Bi K, Zheng Y, Gao F, Dong J, Wang J, Wang Y, Gong W Protein Cell. 2014 Jan 30. PMID:24474195<ref>PMID:24474195</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Arginine--tRNA ligase]] | [[Category: Arginine--tRNA ligase]] | ||
| - | [[Category: Bi, K | + | [[Category: Ecoli]] |
| - | [[Category: Dong, J | + | [[Category: Bi, K]] |
| - | [[Category: Gao, F | + | [[Category: Dong, J]] |
| - | [[Category: Gong, W | + | [[Category: Gao, F]] |
| - | [[Category: Wang, J | + | [[Category: Gong, W]] |
| - | [[Category: Wang, Y | + | [[Category: Wang, J]] |
| - | [[Category: Zheng, Y | + | [[Category: Wang, Y]] |
| + | [[Category: Zheng, Y]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 04:39, 22 December 2014
Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition
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