5ah5: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ah5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_radiobacter_K84 Agrobacterium radiobacter K84] and [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AH5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ah5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_radiobacter_K84 Agrobacterium radiobacter K84] and [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AH5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LSS:5-O-(L-LEUCYLSULFAMOYL)ADENOSINE'>LSS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LSS:5-O-(L-LEUCYLSULFAMOYL)ADENOSINE'>LSS</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5ah5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ah5 OCA], [https://pdbe.org/5ah5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ah5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ah5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ah5 ProSAT]</span></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=5ah5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ah5 OCA], [https://pdbe.org/5ah5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ah5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ah5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ah5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 14:09, 10 January 2024
Crystal structure of the ternary complex of Agrobacterium radiobacter K84 agnB2 LeuRS-tRNA-LeuAMSCrystal structure of the ternary complex of Agrobacterium radiobacter K84 agnB2 LeuRS-tRNA-LeuAMS
Structural highlights
FunctionPublication Abstract from PubMedAntibiotic-producing microbes evolved self-resistance mechanisms to avoid suicide. The biocontrol Agrobacterium radiobacter K84 secretes the Trojan Horse antibiotic agrocin 84 that is selectively transported into the plant pathogen A. tumefaciens and processed into the toxin TM84. We previously showed that TM84 employs a unique tRNA-dependent mechanism to inhibit leucyl-tRNA synthetase (LeuRS), while the TM84-producer prevents self-poisoning by expressing a resistant LeuRS AgnB2. We now identify a mechanism by which the antibiotic-producing microbe resists its own toxin. Using a combination of structural, biochemical and biophysical approaches, we show that AgnB2 evolved structural changes so as to resist the antibiotic by eliminating the tRNA-dependence of TM84 binding. Mutagenesis of key resistance determinants results in mutants adopting an antibiotic-sensitive phenotype. This study illuminates the evolution of resistance in self-immunity genes and provides mechanistic insights into a fascinating tRNA-dependent antibiotic with applications for the development of anti-infectives and the prevention of biocontrol emasculation. Structural characterization of antibiotic self-immunity tRNA synthetase in plant tumour biocontrol agent.,Chopra S, Palencia A, Virus C, Schulwitz S, Temple BR, Cusack S, Reader J Nat Commun. 2016 Oct 7;7:12928. doi: 10.1038/ncomms12928. PMID:27713402[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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