6AHR

Cryo-EM structure of human Ribonuclease P

Summary for 6AHR

• Entry DOI: 10.2210/pdb6ahr/pdb
• EMDB information: 9616 9626
• Descriptor: H1 RNA, Ribonuclease P protein subunit p21, Ribonuclease P protein subunit p40, ... (12 entities in total)
• Functional Keywords: ribonuclease p, rna-protein complex, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 469665.44

Authors

Wu, J.,Niu, S.,Tan, M.,Lan, P.,Lei, M. (deposition date: 2018-08-20, release date: 2018-12-05, Last modification date: 2024-03-27)

Primary citation

Wu, J.,Niu, S.,Tan, M.,Huang, C.,Li, M.,Song, Y.,Wang, Q.,Chen, J.,Shi, S.,Lan, P.,Lei, M.
Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.
Cell, 175:1393-1404.e11, 2018

PubMed Abstract: Ribonuclease (RNase) P is a ubiquitous ribozyme that cleaves the 5' leader from precursor tRNAs. Here, we report cryo-electron microscopy structures of the human nuclear RNase P alone and in complex with tRNA. Human RNase P is a large ribonucleoprotein complex that contains 10 protein components and one catalytic RNA. The protein components form an interlocked clamp that stabilizes the RNA in a conformation optimal for substrate binding. Human RNase P recognizes the tRNA using a double-anchor mechanism through both protein-RNA and RNA-RNA interactions. Structural comparison of the apo and tRNA-bound human RNase P reveals that binding of tRNA induces a local conformational change in the catalytic center, transforming the ribozyme into an active state. Our results also provide an evolutionary model depicting how auxiliary RNA elements in bacterial RNase P, essential for substrate binding, and catalysis, were replaced by the much more complex and multifunctional protein components in higher organisms.

PubMed: 30454648
DOI: 10.1016/j.cell.2018.10.003

Experimental method

ELECTRON MICROSCOPY (3.92 Å)