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| | <StructureSection load='4p3p' size='340' side='right'caption='[[4p3p]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4p3p' size='340' side='right'caption='[[4p3p]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4p3p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P3P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4p3p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P3P FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2CR:(1R,2R)-2-[(2S,4E,6E,8R,9S,11R,13S,15S,16S)-7-CYANO-8,16-DIHYDROXY-9,11,13,15-TETRAMETHYL-18-OXOOXACYCLOOCTADECA-4,6-DIEN-2-YL]CYCLOPENTANECARBOXYLIC+ACID'>2CR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CR:(1R,2R)-2-[(2S,4E,6E,8R,9S,11R,13S,15S,16S)-7-CYANO-8,16-DIHYDROXY-9,11,13,15-TETRAMETHYL-18-OXOOXACYCLOOCTADECA-4,6-DIEN-2-YL]CYCLOPENTANECARBOXYLIC+ACID'>2CR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p3n|4p3n]], [[4p3o|4p3o]]</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=4p3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3p OCA], [https://pdbe.org/4p3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p3p RCSB], [https://www.ebi.ac.uk/pdbsum/4p3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3p ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thrS, b1719, JW1709 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </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=4p3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p3p OCA], [http://pdbe.org/4p3p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p3p RCSB], [http://www.ebi.ac.uk/pdbsum/4p3p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p3p ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SYT_ECOLI SYT_ECOLI]] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184] | + | [https://www.uniprot.org/uniprot/SYT_ECOLI SYT_ECOLI] ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Threonine--tRNA ligase]]
| + | [[Category: Chen K]] |
| - | [[Category: Chen, K]] | + | [[Category: Chen X]] |
| - | [[Category: Chen, X]] | + | [[Category: Fang P]] |
| - | [[Category: Fang, P]] | + | [[Category: Guo M]] |
| - | [[Category: Guo, M]] | + | [[Category: Yu X]] |
| - | [[Category: Yu, X]] | + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Ligase-ligase inhibitor complex]]
| + | |
| - | [[Category: Synthetase]]
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| Structural highlights
Function
SYT_ECOLI ThrS is also a translational repressor protein, it controls the translation of its own gene by binding to its mRNA.[HAMAP-Rule:MF_00184]
Publication Abstract from PubMed
The polyketide natural product borrelidin displays antibacterial, antifungal, antimalarial, anticancer, insecticidal and herbicidal activities through the selective inhibition of threonyl-tRNA synthetase (ThrRS). How borrelidin simultaneously attenuates bacterial growth and suppresses a variety of infections in plants and animals is not known. Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. Thus, borrelidin competes with all three aminoacylation substrates, providing a potent and redundant mechanism to inhibit ThrRS during protein synthesis. These results highlight a surprising natural design to achieve the quadrivalent inhibition of translation through a highly conserved family of enzymes.
Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase.,Fang P, Yu X, Jeong SJ, Mirando A, Chen K, Chen X, Kim S, Francklyn CS, Guo M Nat Commun. 2015 Mar 31;6:6402. doi: 10.1038/ncomms7402. PMID:25824639[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fang P, Yu X, Jeong SJ, Mirando A, Chen K, Chen X, Kim S, Francklyn CS, Guo M. Structural basis for full-spectrum inhibition of translational functions on a tRNA synthetase. Nat Commun. 2015 Mar 31;6:6402. doi: 10.1038/ncomms7402. PMID:25824639 doi:http://dx.doi.org/10.1038/ncomms7402
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