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1h3e

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[[Image:1h3e.gif|left|200px]]<br />
 
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<applet load="1h3e" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h3e, resolution 2.90&Aring;" />
 
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'''TYROSYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH WILD-TYPE TRNATYR(GUA) AND WITH ATP AND TYROSINOL'''<br />
 
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==Overview==
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==Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA) and with ATP and tyrosinol==
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Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked, C-terminal domain of approximately 80 residues, which has hitherto been, disordered in crystal structures of the enzyme. We have determined the, structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal, form in which the C-terminal domain is ordered, and confirm that the fold, is similar to part of the C-terminal domain of ribosomal protein S4. We, have also determined the structure at 2.9 A resolution of the complex of, T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm, of the tRNA and the anti-codon stem, thus recognizing the unique shape of, the tRNA. The anticodon bases have a novel conformation with A-36 stacked, on G-34, and both G-34 and Psi-35 are base-specifically recognized. The, tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA, resembles that of a class II synthetase in being from the major groove, side of the acceptor stem.
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<StructureSection load='1h3e' size='340' side='right'caption='[[1h3e]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] and [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H3E 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]] 2.9&#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=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=TYE:4-[(2S)-2-AMINO-3-HYDROXYPROPYL]PHENOL'>TYE</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=1h3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h3e OCA], [https://pdbe.org/1h3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h3e RCSB], [https://www.ebi.ac.uk/pdbsum/1h3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h3e ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYY_THET2 SYY_THET2] 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) (By similarity).
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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/h3/1h3e_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=1h3e 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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1H3E is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ATP and TYB as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H3E OCA].
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
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==Reference==
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__TOC__
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Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition., Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S, EMBO J. 2002 Jul 15;21(14):3829-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12110594 12110594]
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</StructureSection>
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Thermus thermophilus HB27]]
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[[Category: Cusack, S.]]
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[[Category: Cusack S]]
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[[Category: Kriklivyi, I.]]
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[[Category: Kriklivyi I]]
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[[Category: Tukalo, M.]]
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[[Category: Tukalo M]]
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[[Category: Yaremchuk, A.]]
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[[Category: Yaremchuk A]]
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[[Category: ATP]]
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[[Category: TYB]]
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[[Category: class i aminoacyl-trna synthetase: atp + l-tyrosine + trna(tyr) -> amp + ppi + l-tyrosyl-trna(tyr)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:27:31 2007''
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Current revision

Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA) and with ATP and tyrosinol

PDB ID 1h3e

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