3Q1Q : Structure of a Bacterial Ribonuclease P Holoenzyme in Complex with tRNA

  • Nicholas J. Reiter (Contributor)
  • Amy K. Osterman (Contributor)
  • Alfredo Torres-Larios (Contributor)
  • Kerren K. Swinger (Contributor)
  • Tao Pan (Contributor)
  • Alfonso Mondragon (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.8
Classification:HYDROLASE/RNA
Release Date:2011-03-09
Deposition Date:2010-12-17
Revision Date:2011-07-13
Molecular Weight:154931.39
Macromolecule Type:Protein#RNA
Residue Count:551
Atom Site Count:10155
DOI:10.2210/pdb3q1q/pdb

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‚ÄČkDa 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.
Date made available2011
PublisherRCSB-PDB

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