8vtz: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8vtz is ON HOLD  until Paper Publication
+==Crystal structure of Aquifex aeolicus Trbp111==
+<StructureSection load='8vtz' size='340' side='right'caption='[[8vtz]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8vtz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VTZ 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]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=8vtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vtz OCA], [https://pdbe.org/8vtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vtz RCSB], [https://www.ebi.ac.uk/pdbsum/8vtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vtz 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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8vtz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Aquifex aeolicus]]
+[[Category: Large Structures]]
+[[Category: Umuhire Juru A]]
+[[Category: Zhang J]]