7UO0

E.coli RNaseP Holoenzyme with Mg2+

Summary for 7UO0

• Entry DOI: 10.2210/pdb7uo0/pdb
• EMDB information: 26636
• Descriptor: Ribonuclease P protein component, RNase P RNA, Precursor tRNA substrate G(-1) G(-2), ... (4 entities in total)
• Functional Keywords: ribozyme, protein-rna complex, divalent ion, rna, hydrolase-rna complex, hydrolase/rna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 161627.31

Authors

Huang, W.,Taylor, D.J. (deposition date: 2022-04-12, release date: 2022-09-28, Last modification date: 2024-06-12)

Primary citation

Zhu, J.,Huang, W.,Zhao, J.,Huynh, L.,Taylor, D.J.,Harris, M.E.
Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P.
Nat Commun, 13:5120-5120, 2022

PubMed Abstract: Binding of precursor tRNAs (ptRNAs) by bacterial ribonuclease P (RNase P) involves an encounter complex (ES) that isomerizes to a catalytic conformation (ES*). However, the structures of intermediates and the conformational changes that occur during binding are poorly understood. Here, we show that pairing between the 5' leader and 3'RCCA extending the acceptor stem of ptRNA inhibits ES* formation. Cryo-electron microscopy single particle analysis reveals a dynamic enzyme that becomes ordered upon formation of ES* in which extended acceptor stem pairing is unwound. Comparisons of structures with alternative ptRNAs reveals that once unwinding is completed RNase P primarily uses stacking interactions and shape complementarity to accommodate alternative sequences at its cleavage site. Our study reveals active site interactions and conformational changes that drive molecular recognition by RNase P and lays the foundation for understanding how binding interactions are linked to helix unwinding and catalysis.

PubMed: 36045135
DOI: 10.1038/s41467-022-32843-7

Experimental method

ELECTRON MICROSCOPY (3.4 Å)