3Q1Q

Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA

「3OK7」から置き換えられました

3Q1Q の概要

• エントリーDOI: 10.2210/pdb3q1q/pdb
• 関連するPDBエントリー: 1EHZ 1NBS 1NZ0 1U9S 2A2E 2A64 3Q1R
• 分子名称: RNase P RNA, Ribonuclease P protein component, TRNA (PHE), ... (5 entities in total)
• 機能のキーワード: rnase p, ribozyme, ribonuclease p, trna, pre-trna, tetraloop-receptor, ribose zipper, a-minor interaction, base stacking, intermolecular base pairs, intermolecular rna-rna contacts, rnp, ribonucleoprotein complex, enzyme-product complex, metalloenzyme, rna-metal interactions, shape complementarity, hydrolase-rna complex, endonuclease, hydrolase/rna
• 由来する生物種: Thermotoga maritima; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 154931.39

構造登録者

Reiter, N.J.,Osterman, A.,Torres-Larios, A.,Swinger, K.K.,Pan, T.,Mondragon, A. (登録日: 2010-12-17, 公開日: 2011-03-09, 最終更新日: 2023-09-13)

主引用文献

Reiter, N.J.,Osterman, A.,Torres-Larios, A.,Swinger, K.K.,Pan, T.,Mondragon, A.
Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA.
Nature, 468:784-789, 2010

PubMed Abstract: Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA(Phe). The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA-RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5' leader sequence with and without metal help to identify the 5' substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of catalysis by RNase P.

PubMed: 21076397
DOI: 10.1038/NATURE09516

実験手法

X-RAY DIFFRACTION (3.8 Å)