View source for 9ovc


==Structure of Geobacillus stearothermophilus RNase P ribozyme in 10 mM Mg2+==
<StructureSection load='9ovc' size='340' side='right'caption='[[9ovc]], [[Resolution|resolution]] 2.97&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ovc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OVC 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]] 2.97&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9ovc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ovc OCA], [https://pdbe.org/9ovc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ovc RCSB], [https://www.ebi.ac.uk/pdbsum/9ovc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ovc ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ribonuclease P (RNase P) is an essential metallonuclease found in all three domains of life. However, the structural basis for the ancient RNase P RNA component acting alone as a ribozyme and catalytic metal-ion chemistry remains unknown. We report a series of cryo-EM structures, at resolutions of 2.8-3.5 A, of the Geobacillus stearothermophilus RNase P aporibozyme (apoE) in various states of the catalytic cycle. The formation of both the tetraloop/tetraloop-receptor interaction and the interdigitated double T-loop motif in the substrate-specificity domain facilitates substrate binding. The apoE uses two metal ions for catalysis, suggesting a catalytic mechanism and evolutionary importance of the RNase P ribozyme to function without its protein component. Together, our data portray the regulatory RNA-RNA interfaces, dynamic structures, and cation traffic that confer function to a trans-acting ribozyme.

Structural basis for protein-free catalysis by ribonuclease P ribozyme.,Lee YT, Degenhardt MFS, Skeparnias I, Chen SY, Bhoge BA, Tarasov SG, Dyba MA, Zhang J, Stagno JR, Wang YX Nat Commun. 2026 Apr 15. doi: 10.1038/s41467-026-71597-4. PMID:41986363<ref>PMID:41986363</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9ovc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Large Structures]]
[[Category: Lee Y-T]]
[[Category: Skeparnias I]]
[[Category: Stagno JR]]
[[Category: Wang Y-X]]