1tky

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{{Seed}}
 
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[[Image:1tky.png|left|200px]]
 
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==Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine==
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The line below this paragraph, containing "STRUCTURE_1tky", creates the "Structure Box" on the page.
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<StructureSection load='1tky' size='340' side='right'caption='[[1tky]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1tky]] is a 1 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=1TKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TKY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.48&#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=A3S:SERINE-3-AMINOADENOSINE'>A3S</scene></td></tr>
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{{STRUCTURE_1tky| PDB=1tky | SCENE= }}
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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=1tky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tky OCA], [https://pdbe.org/1tky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tky RCSB], [https://www.ebi.ac.uk/pdbsum/1tky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tky ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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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/tk/1tky_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=1tky 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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The fidelity of aminoacylation of tRNA(Thr) by the threonyl-tRNA synthetase (ThrRS) requires the discrimination of the cognate substrate threonine from the noncognate serine. Misacylation by serine is corrected in a proofreading or editing step. An editing site has been located 39 A away from the aminoacylation site. We report the crystal structures of this editing domain in its apo form and in complex with the serine product, and with two nonhydrolyzable analogs of potential substrates: the terminal tRNA adenosine charged with serine, and seryl adenylate. The structures show how serine is recognized, and threonine rejected, and provide the structural basis for the editing mechanism, a water-mediated hydrolysis of the mischarged tRNA. When the adenylate analog binds in the editing site, a phosphate oxygen takes the place of one of the catalytic water molecules, thereby blocking the reaction. This rules out a correction mechanism that would occur before the binding of the amino acid on the tRNA.
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===Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine===
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Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution.,Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D Mol Cell. 2004 Nov 5;16(3):375-86. PMID:15525511<ref>PMID:15525511</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tky" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15525511}}, adds the Publication Abstract to the page
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15525511 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15525511}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1TKY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKY OCA].
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==Reference==
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Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution., Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D, Mol Cell. 2004 Nov 5;16(3):375-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15525511 15525511]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Threonine--tRNA ligase]]
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[[Category: Bey G]]
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[[Category: Bey, G.]]
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[[Category: Caillet J]]
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[[Category: Caillet, J.]]
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[[Category: Dock-Bregeon AC]]
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[[Category: Dock-Bregeon, A C.]]
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[[Category: Moras D]]
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[[Category: Moras, D.]]
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[[Category: Rees B]]
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[[Category: Rees, B.]]
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[[Category: Torres-Larios A]]
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[[Category: Torres-Larios, A.]]
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[[Category: Ligase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:41:03 2008''
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Current revision

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine

PDB ID 1tky

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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