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

Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.

Structure (London, England : 1993) - 7 Jun 2016

Johansson Renzo, Jonna Venkateswara Rao, Kumar Rohit, Nayeri Niloofar, Lundin Daniel, Sjöberg Britt-Marie, Hofer Anders, Logan Derek T

Abstract excerpt

Ribonucleotide reductases (RNRs) reduce ribonucleotides to deoxyribonucleotides. Their overall activity is stimulated by ATP and downregulated by dATP via a genetically mobile ATP cone domain mediating the formation of oligomeric complexes with varying quaternary structures. The crystal structure and solution X-ray scattering data of a novel dATP-induced homotetramer of the Pseudomonas aeruginosa class I RNR...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Allosteric Regulation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to Crystallography, X-Ray

Share to Models, Molecular

Share to Protein Conformation

Share to Pseudomonas aeruginosa

Share to Ribonucleotide Reductases

Source

Identifiers

PMID: 27133024
DOI: 10.1016/j.str.2016.03.025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.PMID 27133024Read ↗

Solution structure of an ATP-binding RNA aptamer reveals a novel fold.Semantic proximity Read ↗

Evolution of oligomeric state through allosteric pathways that mimic ligand binding.Semantic proximity Read ↗

Functional analysis of the Streptomyces coelicolor NrdR ATP-cone domain: role in nucleotide binding, oligomerization, and DNA interactions.Semantic proximity Read ↗

A structural intermediate pre-organizes the add adenine riboswitch for ligand recognition.Semantic proximity Read ↗

Mutant R1 proteins from Escherichia coli class Ia ribonucleotide reductase with altered responses to dATP inhibition.Semantic proximity Read ↗

Starting a new chapter on class Ia ribonucleotide reductasesSemantic proximity Read ↗

Insights into xanthine riboswitch structure and metal ion-mediated ligand recognition.Semantic proximity Read ↗

Structural insights into recognition of c-di-AMP by the ydaO riboswitch.Semantic proximity Read ↗

Recognition of planar and nonplanar ligands in the malachite green-RNA aptamer complex.Semantic proximity Read ↗

Novel mutator mutants of E. coli nrdAB ribonucleotide reductase: insight into allosteric regulation and control of mutation rates.Semantic proximity Read ↗

Structural aspects for the function of ATP-binding ribonucleopeptide receptors.Semantic proximity Read ↗

How do ADARs bind RNA? New protein‐RNA structures illuminate substrate recognition by the RNA editing ADARsSemantic proximity Read ↗

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