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

Conformational changes of Spo0F along the phosphotransfer pathway.

Journal of bacteriology - 1 Dec 2005

Varughese Kottayil I

Abstract excerpt

Spo0F is a secondary messenger in the sporulation phosphorelay, and its structure has been characterized crystallographically in the apo-state, in the metal-bound state, and in an interacting state with a phosphotransferase. Additionally, the solution structure of the molecule has been characterized by nuclear magnetic resonance techniques in the unliganded state and in complex with beryllofluoride. Spo0F is a...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Fluorides
Share to Nuclear Magnetic Resonance, Biomolecular

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

Share to Phosphorylation

Share to Protein Conformation

Share to Protein Structure, Secondary

Share to Second Messenger Systems

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 16321923
DOI: 10.1128/JB.187.24.8221-8227.2005
PMCID: PMC1316990

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational changes of Spo0F along the phosphotransfer pathway.PMID 16321923Read ↗

Rebuttal: conformational changes of Spo0F along the phosphotransfer pathway.Semantic proximity Read ↗

Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.Semantic proximity Read ↗

Metal fluorides - multi-functional tools for the study of phosphoryl transfer enzymesSemantic proximity Read ↗

Phosphorylation induces subtle structural changes in SpoIIAA, a key regulator of sporulation.Semantic proximity Read ↗

NMR studies of the interactions of SpoIIAA with its partner proteins that regulate sporulation in Bacillus subtilis.Semantic proximity Read ↗

A genetic analysis of Spo0A structure and function.Semantic proximity Read ↗

Backbone resonance assignment of the response regulator protein PhoBNF20D from Escherichia coli.Semantic proximity Read ↗

REGULATION OF THE PHOSPHORELAY AND THE INITIATION OF SPORULATION IN <i>BACILLUS SUBTILIS</i>Semantic proximity Read ↗

Studies of SpoIIAB mutant proteins elucidate the mechanisms that regulate the developmental transcription factor sigmaF in Bacillus subtilis.Semantic proximity Read ↗

Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states.Semantic proximity Read ↗

Bacillus subtilis mutations that alter the pathway of phosphorylation of the anti-anti-sigmaF factor SpoIIAA lead to a Spo- phenotype.Semantic proximity Read ↗

Interaction surface of the Spo0A response regulator with the Spo0E phosphatase.Semantic proximity Read ↗

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