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

Isolated epsilon subunit of Bacillus subtilis F1-ATPase binds ATP.

FEBS letters - 19 Dec 2005

Kato-Yamada Yasuyuki

Abstract excerpt

Previously, we demonstrated ATP binding to the isolated epsilon subunit of F1-ATPase from thermophilic Bacillus PS3 [Kato-Yamada Y., Yoshida M. (2003) J. Biol. Chem. 278, 36013]. However, whether it is a general feature of the epsilon subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled epsilon subunit and nucleotide, it was shown that...

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 Bacillus subtilis
Share to Kinetics

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Plasmids

Share to Protein Conformation

Share to Protein Subunits

Share to Proton-Translocating ATPases

Share to Titrimetry

Source

Identifiers

PMID: 16337201
DOI: 10.1016/j.febslet.2005.11.036

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

Isolated epsilon subunit of Bacillus subtilis F1-ATPase binds ATP.PMID 16337201Read ↗

Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.Semantic proximity Read ↗

Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase.Semantic proximity Read ↗

Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3.Semantic proximity Read ↗

High affinity nucleotide-binding mutant of the ε subunit of thermophilic F1-ATPase.Semantic proximity Read ↗

A single mutation at the catalytic site of TF1-alpha3beta3gamma complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity.Semantic proximity Read ↗

The role of the betaDELSEED-loop of ATP synthase.Semantic proximity Read ↗

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Semantic proximity Read ↗

Mutation of a key residue in the type II secretion system ATPase uncouples ATP hydrolysis from protein translocation.Semantic proximity Read ↗

The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.Semantic proximity Read ↗

Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy.Semantic proximity Read ↗

Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase.Semantic proximity Read ↗

ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.Semantic proximity Read ↗

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