3ts1

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(New page: 200px<br /><applet load="3ts1" size="450" color="white" frame="true" align="right" spinBox="true" caption="3ts1, resolution 2.7&Aring;" /> '''STRUCTURE OF TYROSYL-...)
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[[Image:3ts1.jpg|left|200px]]<br /><applet load="3ts1" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3ts1, resolution 2.7&Aring;" />
 
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'''STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE'''<br />
 
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==Overview==
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==STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE==
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The crystal structure of tyrosyl-tRNA synthetase (EC 6.1.1.1) from, Bacillus stearothermophilus has been refined to a crystallographic, R-factor of 22.6% at 2.3 A resolution using a restrained least-squares, procedure. In the final model the root-mean-square deviation from ideality, for bond distances is 0.018 A and for angle distances is 0.044 A. Each, monomer consists of three domains: an alpha/beta domain (residues 1 to, 220) containing a six-stranded beta-sheet, an alpha-helical domain (248 to, 318) containing five helices, and a disordered C-terminal domain (319 to, 418) for which the electron density is very weak and where it has not been, possible to trace the polypeptide chain. Complexes of the enzyme with the, catalytic intermediate tyrosyl adenylate and the inhibitor tyrosinyl, adenylate have also been refined to R-factors of 23.9% at 2.8 A resolution, and 21.0% at 2.7 A resolution, respectively. Formation of the complexes, results in some crystal cracking, but there is no significant difference, in the conformation of the polypeptide chain of the three structures, described here. The relative orientation of the alpha/beta and, alpha-helical domains is similar to that previously observed for the "A", subunit of a deletion mutant lacking the C-terminal domain. Differences, between these structures are confined to surface loops that are involved, in crystal packing. Tyrosyl adenylate and tyrosinyl adenylate bind in, similar conformations within a deep cleft in the alpha/beta domain. The, tyrosine moiety is in the equivalent position to that occupied by tyrosine, in crystals of the truncated mutant and makes similar strong polar, interactions with the enzyme. The alpha-phosphate group interacts with the, main-chain nitrogen of Asp38. The two hydroxyl groups of the ribose form, strong interactions with the protein. The 2'-hydroxyl group interacts with, the carboxylate of Asp194 and the main-chain nitrogen of Gly192 while the, 3'-hydroxyl interacts with a tightly bound water molecule (Wat326). The, adenine moiety appears to make no significant polar interactions with the, protein. The results of site-directed mutagenesis studies are examined in, the light of these refined structures.
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<StructureSection load='3ts1' size='340' side='right'caption='[[3ts1]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ts1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TS1 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]] 2.7&#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=TYA:PHOSPHORIC+ACID+2-AMINO-3-(4-HYDROXY-PHENYL)-PROPYL+ESTER+ADENOSIN-5YL+ESTER'>TYA</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=3ts1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts1 OCA], [https://pdbe.org/3ts1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ts1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ts1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ts1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYY_GEOSE SYY_GEOSE] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
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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/ts/3ts1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3ts1 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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3TS1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with TYA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3TS1 OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of tyrosyl-tRNA synthetase refined at 2.3 A resolution. Interaction of the enzyme with the tyrosyl adenylate intermediate., Brick P, Bhat TN, Blow DM, J Mol Biol. 1989 Jul 5;208(1):83-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2504923 2504923]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Blow DM]]
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[[Category: Blow, D.M.]]
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[[Category: Brick P]]
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[[Category: Brick, P.]]
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[[Category: Monteilhet C]]
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[[Category: Monteilhet, C.]]
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[[Category: TYA]]
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[[Category: ligase (synthetase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:00:09 2007''
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Current revision

STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE

PDB ID 3ts1

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