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5xaq
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5xaq is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Animalia-specific tRNA deacylase from Mus musculus== | |
| + | <StructureSection load='5xaq' size='340' side='right'caption='[[5xaq]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xaq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</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=5xaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xaq OCA], [https://pdbe.org/5xaq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xaq RCSB], [https://www.ebi.ac.uk/pdbsum/5xaq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xaq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DTD2_MOUSE DTD2_MOUSE] May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine (Potential). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic trans-editing factor, removes D-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNA(Ala). An invariant cross-subunit Gly-cisPro motif forms the mechanistic basis of L-amino acid rejection from the catalytic site. Here, we present the identification of a DTD variant, named ATD (Animalia-specific tRNA deacylase), that harbors a Gly-transPro motif. The cis-to-trans switch causes a "gain of function" through L-chiral selectivity in ATD resulting in the clearing of L-alanine mischarged on tRNA(Thr)(G4*U69) by eukaryotic AlaRS. The proofreading activity of ATD is conserved across diverse classes of phylum Chordata. Animalia genomes enriched in tRNA(Thr)(G4*U69) genes are in strict association with the presence of ATD, underlining the mandatory requirement of a dedicated factor to proofread tRNA misaminoacylation. The study highlights the emergence of ATD during genome expansion as a key event associated with the evolution of Animalia. | ||
| - | + | A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.,Kuncha SK, Mazeed M, Singh R, Kattula B, Routh SB, Sankaranarayanan R Nat Commun. 2018 Feb 6;9(1):511. doi: 10.1038/s41467-017-02204-w. PMID:29410408<ref>PMID:29410408</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5xaq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Kattula B]] | ||
| + | [[Category: Kuncha KS]] | ||
| + | [[Category: Sankarnarayanan R]] | ||
Current revision
Crystal structure of Animalia-specific tRNA deacylase from Mus musculus
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