9OWQ
Structure of Geobacillus stearothermophilus RNase P ribozyme in complex with precursor tRNA with loop-back 5' leader
Summary for 9OWQ
| Entry DOI | 10.2210/pdb9owq/pdb |
| EMDB information | 70940 |
| Descriptor | RNase P RNA (417-MER), precursor tRNA (109-MER), CALCIUM ION (3 entities in total) |
| Functional Keywords | ribozyme, rna, rnase p. |
| Biological source | Geobacillus stearothermophilus More |
| Total number of polymer chains | 2 |
| Total formula weight | 172526.81 |
| Authors | |
| Primary citation | Lee, Y.T.,Degenhardt, M.F.S.,Skeparnias, I.,Chen, S.Y.,Bhoge, B.A.,Tarasov, S.G.,Dyba, M.A.,Zhang, J.,Stagno, J.R.,Wang, Y.X. Structural basis for protein-free catalysis by ribonuclease P ribozyme. Nat Commun, 2026 Cited by PubMed Abstract: 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 Å, 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. PubMed: 41986363DOI: 10.1038/s41467-026-71597-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.78 Å) |
Structure validation
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