8vu0: Difference between revisions
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==Co-crystal structure of Aquifex aeolicus Trbp111 in complex with E. coli tRNA-Ile== | |||
<StructureSection load='8vu0' size='340' side='right'caption='[[8vu0]], [[Resolution|resolution]] 2.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8vu0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VU0 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]] 2.64Å</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=8vu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vu0 OCA], [https://pdbe.org/8vu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vu0 RCSB], [https://www.ebi.ac.uk/pdbsum/8vu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vu0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O66738_AQUAE O66738_AQUAE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The widespread oligonucleotide/oligosaccharide-binding (OB)-fold recognizes diverse substrates from sugars to nucleic acids and proteins, and plays key roles in genome maintenance, transcription, translation, and tRNA metabolism. OB-containing bacterial Trbp and yeast Arc1p proteins are thought to recognize the tRNA elbow or anticodon regions. Here we report a 2.6 A co-crystal structure of Aquifex aeolicus Trbp111 bound to tRNA(Ile), which reveals that Trbp recognizes tRNAs solely by capturing their 3' ends. Structural, mutational, and biophysical analyses show that the Trbp/EMAPII-like OB fold precisely recognizes the single-stranded structure, 3' terminal location, and specific sequence of the 3' CA dinucleotide - a universal feature of mature tRNAs. Arc1p supplements its OB - tRNA 3' end interaction with additional contacts that involve an adjacent basic region and the tRNA body. This study uncovers a previously unrecognized mode of tRNA recognition by an ancient protein fold, and provides insights into protein-mediated tRNA aminoacylation, folding, localization, trafficking, and piracy. | |||
Structural basis of tRNA recognition by the widespread OB fold.,Umuhire Juru A, Ghirlando R, Zhang J Nat Commun. 2024 Jul 29;15(1):6385. doi: 10.1038/s41467-024-50730-1. PMID:39075051<ref>PMID:39075051</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8vu0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aquifex aeolicus]] | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Umuhire Juru A]] | |||
[[Category: Zhang J]] | |||
Latest revision as of 08:42, 7 August 2024
Co-crystal structure of Aquifex aeolicus Trbp111 in complex with E. coli tRNA-IleCo-crystal structure of Aquifex aeolicus Trbp111 in complex with E. coli tRNA-Ile
Structural highlights
FunctionPublication Abstract from PubMedThe widespread oligonucleotide/oligosaccharide-binding (OB)-fold recognizes diverse substrates from sugars to nucleic acids and proteins, and plays key roles in genome maintenance, transcription, translation, and tRNA metabolism. OB-containing bacterial Trbp and yeast Arc1p proteins are thought to recognize the tRNA elbow or anticodon regions. Here we report a 2.6 A co-crystal structure of Aquifex aeolicus Trbp111 bound to tRNA(Ile), which reveals that Trbp recognizes tRNAs solely by capturing their 3' ends. Structural, mutational, and biophysical analyses show that the Trbp/EMAPII-like OB fold precisely recognizes the single-stranded structure, 3' terminal location, and specific sequence of the 3' CA dinucleotide - a universal feature of mature tRNAs. Arc1p supplements its OB - tRNA 3' end interaction with additional contacts that involve an adjacent basic region and the tRNA body. This study uncovers a previously unrecognized mode of tRNA recognition by an ancient protein fold, and provides insights into protein-mediated tRNA aminoacylation, folding, localization, trafficking, and piracy. Structural basis of tRNA recognition by the widespread OB fold.,Umuhire Juru A, Ghirlando R, Zhang J Nat Commun. 2024 Jul 29;15(1):6385. doi: 10.1038/s41467-024-50730-1. PMID:39075051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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