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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]] 1.93Å' scene=''> | | <StructureSection load='4rrg' size='340' side='right'caption='[[4rrg]], [[Resolution|resolution]] 1.93Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4rrg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RRG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RRG FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4rrg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RRG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RRG FirstGlance]. <br> |
| </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> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</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='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> |
| <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'>[https://proteopedia.org/fgij/fg.htm?mol=4rrg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rrg OCA], [https://pdbe.org/4rrg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rrg RCSB], [https://www.ebi.ac.uk/pdbsum/4rrg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rrg ProSAT]</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;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/SYT_METJA SYT_METJA] |
| 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>
| | ==See Also== |
| | | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4rrg" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Threonine--tRNA ligase]] | | [[Category: Large Structures]] |
| [[Category: Ahmad, S]] | | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| [[Category: Kamarthapu, V]] | | [[Category: Ahmad S]] |
| [[Category: Sankaranarayanan, R]]
| | [[Category: Kamarthapu V]] |
| [[Category: Yerabham, A S.K]]
| | [[Category: Sankaranarayanan R]] |
| [[Category: Dtd-like fold]] | | [[Category: Yerabham ASK]] |
| [[Category: Ligase]] | |
| [[Category: Proofreading]] | |