View source for 7ur5


==allo-tRNAUTu1 in the A, P, and E sites of the E. coli ribosome==
<StructureSection load='7ur5' size='340' side='right'caption='[[7ur5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ur5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Metagenome Metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UR5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#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=7ur5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ur5 OCA], [https://pdbe.org/7ur5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ur5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ur5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ur5 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribosomes are remarkable in their malleability to accept diverse aminoacyl-tRNA substrates from both the same organism and other organisms or domains of life. This is a critical feature of the ribosome that allows the use of orthogonal translation systems for genetic code expansion. Optimization of these orthogonal translation systems generally involves focusing on the compatibility of the tRNA, aminoacyl-tRNA synthetase, and a non-canonical amino acid with each other. As we expand the diversity of tRNAs used to include non-canonical structures, the question arises as to the tRNA suitability on the ribosome. Specifically, we investigated the ribosomal translation of allo-tRNAUTu1, a uniquely shaped (9/3) tRNA exploited for site-specific selenocysteine insertion, using single-molecule fluorescence. With this technique we identified ribosomal disassembly occurring from translocation of allo-tRNAUTu1 from the A to the P site. Using cryo-EM to capture the tRNA on the ribosome, we pinpointed a distinct tertiary interaction preventing fluid translocation. Through a single nucleotide mutation, we disrupted this tertiary interaction and relieved the translation roadblock. With the continued diversification of genetic code expansion, our work highlights a targeted approach to optimize translation by distinct tRNAs as they move through the ribosome.

Uncovering translation roadblocks during the development of a synthetic tRNA.,Prabhakar A, Krahn N, Zhang J, Vargas-Rodriguez O, Krupkin M, Fu Z, Acosta-Reyes FJ, Ge X, Choi J, Crnkovic A, Ehrenberg M, Puglisi EV, Soll D, Puglisi J Nucleic Acids Res. 2022 Oct 14;50(18):10201-10211. doi: 10.1093/nar/gkac576. PMID:35882385<ref>PMID:35882385</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ur5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Metagenome]]
[[Category: Acosta-Reyes FJ]]
[[Category: Choi J]]
[[Category: Crnkovic A]]
[[Category: Ehrenberg M]]
[[Category: Fu Z]]
[[Category: Ge X]]
[[Category: Krahn N]]
[[Category: Krupkin M]]
[[Category: Prabhakar A]]
[[Category: Puglisi J]]
[[Category: Soll D]]
[[Category: Vargas-Rodriguez O]]
[[Category: Viani Puglisi E]]
[[Category: Zhang J]]