View source for 9mkl


==canavanyl-tRNAArg deacylase (CtdA)==
<StructureSection load='9mkl' size='340' side='right'caption='[[9mkl]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9mkl]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MKL 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]] 1.98&#8491;</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=9mkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mkl OCA], [https://pdbe.org/9mkl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mkl RCSB], [https://www.ebi.ac.uk/pdbsum/9mkl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mkl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0W4F7L0_SALER A0A0W4F7L0_SALER] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aminoacyl-tRNA deacylases safeguard the accurate translation of the genetic code by hydrolyzing incorrectly synthesized aminoacyl-tRNAs. Canavanyl-tRNA deacylase (CtdA) was recently shown to protect cells against the toxicity of canavanine (Can), a nonproteinogenic amino acid synthesized and accumulated by leguminous plants. In most organisms, Can is ligated to tRNAArg, causing translation of arginine codons with Can. CtdA prevents Can toxicity by hydrolyzing canavanyl-tRNAArg. Here, we investigated the function, structure, substrate specificity, phylogenetic distribution, and evolution of CtdA. We show that CtdA is essential for preventing Can cytotoxicity in Salmonella enterica, and its heterologous expression can also protect Escherichia coli. By determining the structure of CtdA, we identified its putative binding pocket and residues that modulate enzymatic activity and specificity. We also found that CtdA displays robust specificity for the canavanyl moiety, a feature that contributes to maintaining arginyl-tRNAArg levels unaffected. Finally, we showed that despite their structural homology, CtdA and the aminoacyl-tRNA hydrolytic domain of phenylalanyl-tRNA synthetase are functionally and evolutionarily divergent. Collectively, these results substantially expand our understanding of the CtdA family, providing new insights into its structure, function, and evolution. This work also highlights the diverse mechanisms, unique to each organism, that ensure faithful translation of the genetic code.

Mechanistic and evolutionary insights into a family of aminoacyl-tRNA deacylases that protects against canavanine toxicity.,Maldonado JS, Sepulveda S, Karthikeyan S, Shirakawa KT, Merced I, Radecki AA, Douglas J, Peti W, Page R, Vargas-Rodriguez O Nucleic Acids Res. 2025 Sep 5;53(17):gkaf922. doi: 10.1093/nar/gkaf922. PMID:40973455<ref>PMID:40973455</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9mkl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica]]
[[Category: Page R]]
[[Category: Peti W]]
[[Category: Shirakawa K]]