3zgz
From Proteopedia
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| - | [[ | + | ==Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and toxic moiety from agrocin 84 (TM84) in aminoacylation-like conformation== |
| + | <StructureSection load='3zgz' size='340' side='right' caption='[[3zgz]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3zgz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZGZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=84T:[(2S,4S,5R)-5-(6-AMINOPURIN-9-YL)-4-OXIDANYL-OXOLAN-2-YL]METHOXY-N-[(2S,3R)-4-METHYL-2,3-BIS(OXIDANYL)PENTANOYL]PHOSPHONAMIDIC+ACID'>84T</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucine--tRNA_ligase Leucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.4 6.1.1.4] </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=3zgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zgz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zgz RCSB], [http://www.ebi.ac.uk/pdbsum/3zgz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Leucyl-tRNA synthetases (LeuRSs) have an essential role in translation and are promising targets for antibiotic development. Agrocin 84 is a LeuRS inhibitor produced by the biocontrol agent Agrobacterium radiobacter K84 that targets pathogenic strains of A. tumefaciens, the causative agent of plant tumours. Agrocin 84 acts as a molecular Trojan horse and is processed inside the pathogen into a toxic moiety (TM84). Here we show using crystal structure, thermodynamic and kinetic analyses, that this natural antibiotic employs a unique and previously undescribed mechanism to inhibit LeuRS. TM84 requires tRNA(Leu) for tight binding to the LeuRS synthetic active site, unlike any previously reported inhibitors. TM84 traps the enzyme-tRNA complex in a novel 'aminoacylation-like' conformation, forming novel interactions with the KMSKS loop and the tRNA 3'-end. Our findings reveal an intriguing tRNA-dependent inhibition mechanism that may confer a distinct evolutionary advantage in vivo and inform future rational antibiotic design. | ||
| - | + | Plant tumour biocontrol agent employs a tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase.,Chopra S, Palencia A, Virus C, Tripathy A, Temple BR, Velazquez-Campoy A, Cusack S, Reader JS Nat Commun. 2013 Jan 29;4:1417. doi: 10.1038/ncomms2421. PMID:23361008<ref>PMID:23361008</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Leucine--tRNA ligase]] | [[Category: Leucine--tRNA ligase]] | ||
| - | [[Category: Chopra, S | + | [[Category: Chopra, S]] |
| - | [[Category: Cusack, S | + | [[Category: Cusack, S]] |
| - | [[Category: Palencia, A | + | [[Category: Palencia, A]] |
| - | [[Category: Reader, J S | + | [[Category: Reader, J S]] |
| - | [[Category: Temple, B R | + | [[Category: Temple, B R]] |
| - | [[Category: Tripathy, A | + | [[Category: Tripathy, A]] |
| - | [[Category: Velazquez-Campoy, A | + | [[Category: Velazquez-Campoy, A]] |
| - | [[Category: Virus, C | + | [[Category: Virus, C]] |
[[Category: Class i aminoacyl-trna synthetase]] | [[Category: Class i aminoacyl-trna synthetase]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Ligase-rna complex]] | [[Category: Ligase-rna complex]] | ||
[[Category: Protein biosynthesis]] | [[Category: Protein biosynthesis]] | ||
Revision as of 09:42, 4 January 2015
Ternary complex of E. coli leucyl-tRNA synthetase, tRNA(leu) and toxic moiety from agrocin 84 (TM84) in aminoacylation-like conformation
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