5xaq

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m (Protected "5xaq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5xaq is ON HOLD until Paper Publication
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==Crystal structure of Animalia-specific tRNA deacylase from Mus musculus==
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<StructureSection load='5xaq' size='340' side='right'caption='[[5xaq]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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='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>
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</table>
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== Function ==
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5xaq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Kattula B]]
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[[Category: Kuncha KS]]
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[[Category: Sankarnarayanan R]]

Current revision

Crystal structure of Animalia-specific tRNA deacylase from Mus musculus

PDB ID 5xaq

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