9OY4
Structure of Geobacillus stearothermophilus RNase P ribozyme tetraloop mutant (sub-conformation 3)
Summary for 9OY4
| Entry DOI | 10.2210/pdb9oy4/pdb |
| EMDB information | 70996 |
| Descriptor | RNase P RNA component tetraloop mutant, CALCIUM ION (2 entities in total) |
| Functional Keywords | ribozyme, rna, rnase p |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 135997.58 |
| 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 (3.11 Å) |
Structure validation
Download full validation report
