Structure and catalytic function in ribonuclease P.
Multiple magnesium ions in the ribonuclease P reaction mechanism.
A kinetic mechanism for cleavage of precursor tRNA(Asp) catalyzed by the RNA component of Bacillus subtilis ribonuclease P.
Identification of phosphates involved in catalysis by the ribozyme RNase P RNA.
The NMR structure of 31mer RNA domain of Escherichia coli RNase P RNA using its non-uniformly deuterium labelled counterpart [the 'NMR-window' concept].
Ribonuclease P catalysis requires Mg2+ coordinated to the pro-RP oxygen of the scissile bond.
Analysis of the functional role of conserved residues in the protein subunit of ribonuclease P from Escherichia coli.
Identification by modification-interference of purine N-7 and ribose 2'-OH groups critical for catalysis by bacterial ribonuclease P.
Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using electron paramagnetic resonance spectroscopy.
In vitro analysis of processing at the 3'-end of precursors of M1 RNA, the catalytic subunit of Escherichia coli RNase P: multiple pathways and steps for the processing.
Effects of terminal deletions in C5 protein on promoting RNase P catalysis.
Mg2+-dependent compaction and folding of yeast tRNAPhe and the catalytic domain of the B. subtilis RNase P RNA determined by small-angle X-ray scattering.
Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-Fe.
The structure of ribonuclease P protein from Staphylococcus aureus reveals a unique binding site for single-stranded RNA.
Solution structure and metal-ion binding of the P4 element from bacterial RNase P RNA.
Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein.
Correlation between processing efficiency for ribonuclease P minimal substrates and conformation of the nucleotide -1 at the cleavage position.
Protein cofactor-dependent acquisition of novel catalytic activity by the RNase P ribonucleoprotein of E. coli.
Monitoring the structure of Escherichia coli RNase P RNA in the presence of various divalent metal ions.
Modular construction for function of a ribonucleoprotein enzyme: the catalytic domain of Bacillus subtilis RNase P complexed with B. subtilis RNase P protein.
NAIM and site-specific functional group modification analysis of RNase P RNA: magnesium dependent structure within the conserved P1-P4 multihelix junction contributes to catalysis.
Evidence for a polynuclear metal ion binding site in the catalytic domain of ribonuclease P RNA.
Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA.
Structure of the UGAGAU hexaloop that braces Bacillus RNase P for action.
Elucidation of structure-function relationships in the protein subunit of bacterial RNase P using a genetic complementation approach.
Specific phosphorothioate substitutions probe the active site of Bacillus subtilis ribonuclease P.
Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P.
Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme.
Crystal structure of the specificity domain of ribonuclease P.
High-resolution structure of RNase P protein from Thermotoga maritima.
Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P.
Change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy.
This enzyme is a ribozyme, which is composed of two RNA components (a catalytic component and a specificity domain), and a protein subunit. "Protein C5" is another synonym of the protein subunit. The tertiary structures of the catalytic doman of the RNA component has not been solved yet, whereas the structures of the specificity domain (PDB;1nbs, 1nxl) have been elucidated (see [30]).