6AHV

Crystal structure of human RPP40

6AHV の概要

• エントリーDOI: 10.2210/pdb6ahv/pdb
• 関連するPDBエントリー: 6AHR
• 分子名称: Ribonuclease P protein subunit p40 (2 entities in total)
• 機能のキーワード: rnase p, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41884.84

構造登録者

Wu, J.,Niu, S.,Tan, M.,Lan, P.,Lei, M. (登録日: 2018-08-20, 公開日: 2018-12-05, 最終更新日: 2024-03-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)