Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:4.21
Classification:HYDROLASE/RNA
Release Date:2011-03-09
Deposition Date:2010-12-17
Revision Date:2011-07-13
Molecular Weight:157026.17
Macromolecule Type:Protein#RNA
Residue Count:558
Atom Site Count:10186
DOI:10.2210/pdb3q1r/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 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.
Resolution:4.21
Classification:HYDROLASE/RNA
Release Date:2011-03-09
Deposition Date:2010-12-17
Revision Date:2011-07-13
Molecular Weight:157026.17
Macromolecule Type:Protein#RNA
Residue Count:558
Atom Site Count:10186
DOI:10.2210/pdb3q1r/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 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.
| Date made available | 2011 |
|---|---|
| Publisher | RCSB-PDB |