4rrg: Difference between revisions

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==Editing domain of threonyl-tRNA synthetase from Methanococcus jannaschii with L-Thr3AA==
==Editing domain of threonyl-tRNA synthetase from Methanococcus jannaschii with L-Thr3AA==
<StructureSection load='4rrg' size='340' side='right' caption='[[4rrg]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='4rrg' size='340' side='right' caption='[[4rrg]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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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]], [[4rrh|4rrh]], [[4rri|4rri]], [[4rrj|4rrj]], [[4rrk|4rrk]], [[4rrl|4rrl]], [[4rrm|4rrm]], [[4rrq|4rrq]], [[4rrr|4rrr]]</td></tr>
<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]], [[4rrh|4rrh]], [[4rri|4rri]], [[4rrj|4rrj]], [[4rrk|4rrk]], [[4rrl|4rrl]], [[4rrm|4rrm]], [[4rrq|4rrq]], [[4rrr|4rrr]]</td></tr>
<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>
<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>
<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=4rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rrg RCSB], [http://www.ebi.ac.uk/pdbsum/4rrg PDBsum]</span></td></tr>
<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=4rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrg OCA], [http://pdbe.org/4rrg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rrg RCSB], [http://www.ebi.ac.uk/pdbsum/4rrg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rrg ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4rrg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 16:25, 19 April 2017

Editing domain of threonyl-tRNA synthetase from Methanococcus jannaschii with L-Thr3AAEditing domain of threonyl-tRNA synthetase from Methanococcus jannaschii with L-Thr3AA

Structural highlights

4rrg is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Threonine--tRNA ligase, with EC number 6.1.1.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Ahmad S, Muthukumar S, Kuncha SK, Routh SB, Yerabham AS, Hussain T, Kamarthapu V, Kruparani SP, Sankaranarayanan R. Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme. Nat Commun. 2015 Jun 26;6:7552. doi: 10.1038/ncomms8552. PMID:26113036 doi:http://dx.doi.org/10.1038/ncomms8552

4rrg, resolution 1.93Å

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