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4rrr

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==K121M mutant of N-terminal editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi with L-Thr3AA==
==K121M mutant of N-terminal editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi with L-Thr3AA==
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<StructureSection load='4rrr' size='340' side='right' caption='[[4rrr]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4rrr' size='340' side='right'caption='[[4rrr]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rrr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RRR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_abyssi_GE5 Pyrococcus abyssi GE5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RRR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3T:3-DEOXY-3-(L-THREONYLAMINO)ADENOSINE'>A3T</scene></td></tr>
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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]] 1.86&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rr6|4rr6]], [[4rr7|4rr7]], [[4rr8|4rr8]], [[4rr9|4rr9]], [[4rra|4rra]], [[4rrb|4rrb]], [[4rrc|4rrc]], [[4rrd|4rrd]], [[4rrf|4rrf]], [[4rrg|4rrg]], [[4rrh|4rrh]], [[4rri|4rri]], [[4rrj|4rrj]], [[4rrk|4rrk]], [[4rrl|4rrl]], [[4rrm|4rrm]], [[4rrq|4rrq]]</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=A3T:3-DEOXY-3-(L-THREONYLAMINO)ADENOSINE'>A3T</scene></td></tr>
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<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>
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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=4rrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrr OCA], [https://pdbe.org/4rrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rrr RCSB], [https://www.ebi.ac.uk/pdbsum/4rrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rrr ProSAT]</span></td></tr>
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<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=4rrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rrr RCSB], [http://www.ebi.ac.uk/pdbsum/4rrr PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SYT_PYRAB SYT_PYRAB]
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Proofreading modules of aminoacyl-tRNA synthetases are responsible for enforcing a high fidelity during translation of the genetic code. They use strategically positioned side chains for specifically targeting incorrect aminoacyl-tRNAs. Here, we show that a unique proofreading module possessing a D-aminoacyl-tRNA deacylase fold does not use side chains for imparting specificity or for catalysis, the two hallmark activities of enzymes. We show, using three distinct archaea, that a side-chain-stripped recognition site is fully capable of solving a subtle discrimination problem. While biochemical probing establishes that RNA plays the catalytic role, mechanistic insights from multiple high-resolution snapshots reveal that differential remodelling of the catalytic core at the RNA-peptide interface provides the determinants for correct proofreading activity. The functional crosstalk between RNA and protein elucidated here suggests how primordial enzyme functions could have emerged on RNA-peptide scaffolds before recruitment of specific side chains.
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Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.,Ahmad S, Muthukumar S, Kuncha SK, Routh SB, Yerabham AS, Hussain T, Kamarthapu V, Kruparani SP, Sankaranarayanan R Nat Commun. 2015 Jun 26;6:7552. doi: 10.1038/ncomms8552. PMID:26113036<ref>PMID:26113036</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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==See Also==
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</div>
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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__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Threonine--tRNA ligase]]
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[[Category: Large Structures]]
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[[Category: Hussain, T]]
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[[Category: Pyrococcus abyssi GE5]]
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[[Category: Kamarthapu, V]]
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[[Category: Hussain T]]
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[[Category: Sankaranarayanan, R]]
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[[Category: Kamarthapu V]]
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[[Category: Dtd-like fold]]
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[[Category: Sankaranarayanan R]]
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[[Category: Ligase]]
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[[Category: Proofreading]]
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Current revision

K121M mutant of N-terminal editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi with L-Thr3AA

PDB ID 4rrr

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