9ov6

Structure of Geobacillus stearothermophilus RNase P ribozyme sub-conformation 1

spinqualitylabelsall models 9ov6, resolution 3.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ov6 is a 1 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.46Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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