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-Structure paper
| Title | Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 2617, Year 2019 |
| Publish date | Jun 13, 2019 |
Authors | Futang Wan / Qianmin Wang / Jing Tan / Ming Tan / Juan Chen / Shaohua Shi / Pengfei Lan / Jian Wu / Ming Lei / ![]() |
| 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 ...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. |
External links | Nat Commun / PubMed:31197137 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.3 - 4.6 Å |
| Structure data | EMDB-30036: cryo-EM structure of archaeal Ribonuclease P |
| Chemicals | ![]() ChemComp-ZN: |
| Source |
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Keywords | RNA BINDING PROTEIN/RNA / Ribonuclease P / RNA-protein complex / RNA BINDING PROTEIN-RNA complex |
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methanocaldococcus jannaschii (archaea)
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