Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning.

RNA (New York, N.Y.) - 1 Aug 2006

Christian Eric L, Smith Kari M J, Perera Nicholas, Harris Michael E

Abstract excerpt

Although helix P4 in the catalytic domain of the RNase P ribozyme is known to coordinate magnesium ions important for activity, distinguishing between direct and indirect roles in catalysis has been difficult. Here, we provide evidence for an indirect role in catalysis by showing that while the universally conserved bulge of helix P4 is positioned 5 nt downstream of the cleavage site, changes in its structure can...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cadmium
Share to Catalysis
Share to Magnesium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Metals

Share to Phosphates

Share to Ribonuclease P

Share to RNA, Catalytic

Share to RNA Precursors

Source

Open in PubMed Open full text

Identifiers

PMID: 16822954
DOI: 10.1261/rna.158606
PMCID: PMC1524898

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The P4 metal binding site in RNase P RNA affects active site metal affinity through substrate positioning.PMID 16822954Read ↗

Conservation of helical structure contributes to functional metal ion interactions in the catalytic domain of ribonuclease P RNA.Semantic proximity Read ↗

G350 of Escherichia coli RNase P RNA contributes to Mg2+ binding near the active site of the enzyme.Semantic proximity Read ↗

The RNR motif of B. subtilis RNase P protein interacts with both PRNA and pre-tRNA to stabilize an active conformer.Semantic proximity Read ↗

In vitro selection for altered divalent metal specificity in the RNase P RNA.Semantic proximity Read ↗

NMR and XAS reveal an inner-sphere metal binding site in the P4 helix of the metallo-ribozyme ribonuclease P.Semantic proximity Read ↗

Importance of the +73/294 interaction in Escherichia coli RNase P RNA substrate complexes for cleavage and metal ion coordination.Semantic proximity Read ↗

The pre-tRNA nucleotide base and 2'-hydroxyl at N(-1) contribute to fidelity in tRNA processing by RNase P.Semantic proximity Read ↗

In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain.Semantic proximity Read ↗

Metal ion cooperativity in ribozyme cleavage of RNA.Semantic proximity Read ↗

Recognition of the 5' leader of pre-tRNA substrates by the active site of ribonuclease P.Semantic proximity Read ↗

Structural basis of the enhanced stability of a mutant ribozyme domain and a detailed view of RNA--solvent interactions.Semantic proximity Read ↗

A single metal ion plays structural and chemical roles in an aminoacyl-transferase ribozyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.