1jzs

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(New page: 200px<br /><applet load="1jzs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jzs, resolution 2.5&Aring;" /> '''Isoleucyl-tRNA synthe...)
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[[Image:1jzs.gif|left|200px]]<br /><applet load="1jzs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jzs, resolution 2.5&Aring;" />
 
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'''Isoleucyl-tRNA synthetase Complexed with mupirocin'''<br />
 
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==Overview==
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==Isoleucyl-tRNA synthetase Complexed with mupirocin==
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An analogue of isoleucyl-adenylate (Ile-AMS) potently inhibits the, isoleucyl-tRNA synthetases (IleRSs) from the three primary kingdoms, whereas the antibiotic mupirocin inhibits only the eubacterial and, archaeal IleRSs, but not the eukaryotic enzymes, and therefore is, clinically used against methicillin-resistant Staphylococcus aureus. We, determined the crystal structures of the IleRS from the thermophilic, eubacterium, Thermus thermophilus, in complexes with Ile-AMS and mupirocin, at 3.0- and 2.5-A resolutions, respectively. A structural comparison of, the IleRS.Ile-AMS complex with the adenylate complexes of other, aminoacyl-tRNA synthetases revealed the common recognition mode of, aminoacyl-adenylate by the class I aminoacyl-tRNA synthetases. The Ile-AMS, and mupirocin, which have significantly different chemical structures, are, recognized by many of the same amino acid residues of the IleRS, suggesting that the antibiotic inhibits the enzymatic activity by blocking, the binding site of the high energy intermediate, Ile-AMP. In contrast, the two amino acid residues that concomitantly recognize Ile-AMS and, mupirocin are different between the eubacterial/archaeal IleRSs and the, eukaryotic IleRSs. Mutagenic analyses revealed that the replacement of the, two residues significantly changed the sensitivity to mupirocin.
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<StructureSection load='1jzs' size='340' side='right'caption='[[1jzs]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jzs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRC:MUPIROCIN'>MRC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzs OCA], [https://pdbe.org/1jzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzs RCSB], [https://www.ebi.ac.uk/pdbsum/1jzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzs ProSAT], [https://www.topsan.org/Proteins/RSGI/1jzs TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYI_THET8 SYI_THET8] Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile) (By similarity).[HAMAP-Rule:MF_02003]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jz/1jzs_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jzs ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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An analogue of isoleucyl-adenylate (Ile-AMS) potently inhibits the isoleucyl-tRNA synthetases (IleRSs) from the three primary kingdoms, whereas the antibiotic mupirocin inhibits only the eubacterial and archaeal IleRSs, but not the eukaryotic enzymes, and therefore is clinically used against methicillin-resistant Staphylococcus aureus. We determined the crystal structures of the IleRS from the thermophilic eubacterium, Thermus thermophilus, in complexes with Ile-AMS and mupirocin at 3.0- and 2.5-A resolutions, respectively. A structural comparison of the IleRS.Ile-AMS complex with the adenylate complexes of other aminoacyl-tRNA synthetases revealed the common recognition mode of aminoacyl-adenylate by the class I aminoacyl-tRNA synthetases. The Ile-AMS and mupirocin, which have significantly different chemical structures, are recognized by many of the same amino acid residues of the IleRS, suggesting that the antibiotic inhibits the enzymatic activity by blocking the binding site of the high energy intermediate, Ile-AMP. In contrast, the two amino acid residues that concomitantly recognize Ile-AMS and mupirocin are different between the eubacterial/archaeal IleRSs and the eukaryotic IleRSs. Mutagenic analyses revealed that the replacement of the two residues significantly changed the sensitivity to mupirocin.
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==About this Structure==
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Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase.,Nakama T, Nureki O, Yokoyama S J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. PMID:11584022<ref>PMID:11584022</ref>
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1JZS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN and MRC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isoleucine--tRNA_ligase Isoleucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.5 6.1.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JZS OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase., Nakama T, Nureki O, Yokoyama S, J Biol Chem. 2001 Dec 14;276(50):47387-93. Epub 2001 Oct 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11584022 11584022]
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</div>
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[[Category: Isoleucine--tRNA ligase]]
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<div class="pdbe-citations 1jzs" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Nakama, T.]]
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[[Category: Nureki, O.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Yokoyama, S.]]
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[[Category: MRC]]
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[[Category: ZN]]
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[[Category: aminoacyl-trna synthetase]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:43:40 2007''
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermus thermophilus]]
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[[Category: Nakama T]]
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[[Category: Nureki O]]
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[[Category: Yokoyama S]]

Current revision

Isoleucyl-tRNA synthetase Complexed with mupirocin

PDB ID 1jzs

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