6K0B
cryo-EM structure of archaeal Ribonuclease P with mature tRNA
6K0B の概要
エントリーDOI | 10.2210/pdb6k0b/pdb |
関連するPDBエントリー | 6K0A |
EMDBエントリー | 9900 |
分子名称 | Ribonuclease P protein component 2, Ribonuclease P protein component 3, Ribonuclease P protein component 1, ... (8 entities in total) |
機能のキーワード | ribonuclease p, rna-protein complex, rna binding protein-rna complex, rna binding protein/rna |
由来する生物種 | Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) 詳細 |
タンパク質・核酸の鎖数 | 14 |
化学式量合計 | 385703.68 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 31197137DOI: 10.1038/s41467-019-10496-3 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.3 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード