3Q1Q | pdb_00003q1q

Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA.

(2010) Nature 468: 784-789

• PubMed: 21076397 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/nature09516
• Primary Citation of Related Structures:  
  3Q1Q, 3Q1R


• 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.

   View More

---

Organizational Affiliation: 

Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.