6K0B

cryo-EM structure of archaeal Ribonuclease P with mature tRNA

Summary for 6K0B

• Entry DOI: 10.2210/pdb6k0b/pdb
• Related: 6K0A
• EMDB information: 9900
• Descriptor: Ribonuclease P protein component 2, Ribonuclease P protein component 3, Ribonuclease P protein component 1, ... (8 entities in total)
• Functional Keywords: ribonuclease p, rna-protein complex, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440); More
• Total number of polymer chains: 14
• Total formula weight: 385703.68

Authors

Wan, F.,Lan, P.,Wu, J.,Lei, M. (deposition date: 2019-05-05, release date: 2019-06-19, Last modification date: 2024-03-27)

Primary citation

Wan, F.,Wang, Q.,Tan, J.,Tan, M.,Chen, J.,Shi, S.,Lan, P.,Wu, J.,Lei, M.
Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.
Nat Commun, 10:2617-2617, 2019

PubMed Abstract: Ribonuclease P (RNase P) is an essential ribozyme responsible for tRNA 5' maturation. Here we report the cryo-EM structures of Methanocaldococcus jannaschii (Mja) RNase P holoenzyme alone and in complex with a tRNA substrate at resolutions of 4.6 Å and 4.3 Å, respectively. The structures reveal that the subunits of MjaRNase P are strung together to organize the holoenzyme in a dimeric conformation required for efficient catalysis. The structures also show that archaeal RNase P is a functional chimera of bacterial and eukaryal RNase Ps that possesses bacterial-like two RNA-based anchors and a eukaryal-like protein-aided stabilization mechanism. The 3'-RCCA sequence of tRNA, which is a key recognition element for bacterial RNase P, is dispensable for tRNA recognition by MjaRNase P. The overall organization of MjaRNase P, particularly within the active site, is similar to those of bacterial and eukaryal RNase Ps, suggesting a universal catalytic mechanism for all RNase Ps.

PubMed: 31197137
DOI: 10.1038/s41467-019-10496-3

Experimental method

ELECTRON MICROSCOPY (4.3 Å)