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| | ==Crystal structure of Animalia-specific tRNA deacylase from Mus musculus== | | ==Crystal structure of Animalia-specific tRNA deacylase from Mus musculus== |
| - | <StructureSection load='5xaq' size='340' side='right' caption='[[5xaq]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='5xaq' size='340' side='right'caption='[[5xaq]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xaq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XAQ FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dtd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 1.86Å</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=5xaq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xaq OCA], [http://pdbe.org/5xaq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xaq RCSB], [http://www.ebi.ac.uk/pdbsum/5xaq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xaq ProSAT]</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=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> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Kattula, B]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kuncha, K S]] | + | [[Category: Kattula B]] |
| - | [[Category: Sankarnarayanan, R]] | + | [[Category: Kuncha KS]] |
| - | [[Category: Deacylase]] | + | [[Category: Sankarnarayanan R]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Trna]]
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| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kuncha SK, Mazeed M, Singh R, Kattula B, Routh SB, Sankaranarayanan R. A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia. Nat Commun. 2018 Feb 6;9(1):511. doi: 10.1038/s41467-017-02204-w. PMID:29410408 doi:http://dx.doi.org/10.1038/s41467-017-02204-w
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