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

A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase.

The Journal of biological chemistry - 9 Nov 2012

Sunamura Ei-Ichiro, Konno Hiroki, Imashimizu Mari, Mochimaru Mari, Hisabori Toru

Abstract excerpt

The central shaft of the catalytic core of ATP synthase, the γ subunit consists of a coiled-coil structure of N- and C-terminal α-helices, and a globular domain. The γ subunit of cyanobacterial and chloroplast ATP synthase has a unique 30-40-amino acid insertion within the globular domain. We recently prepared the insertion-removed α(3)β(3)γ complex of cyanobacterial ATP synthase (Sunamura, E., Konno, H.,...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Adenosine Triphosphate

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

Share to Chloroplasts

Share to Cyanobacteria

Share to Hydrolysis

Share to Molecular Conformation

Share to Oxidation-Reduction

Share to Proton-Translocating ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 23012354
DOI: 10.1074/jbc.M112.395053
PMCID: PMC3493913

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

A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase.PMID 23012354Read ↗

Redox regulation of CF1-ATPase involves interplay between the γ-subunit neck region and the turn region of the βDELSEED-loop.Semantic proximity Read ↗

Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase.Semantic proximity Read ↗

C-Terminal mutations in the chloroplast ATP synthase gamma subunit impair ATP synthesis and stimulate ATP hydrolysis.Semantic proximity Read ↗

Mutations on the N-terminal edge of the DELSEED loop in either the α or β subunit of the mitochondrial F1-ATPase enhance ATP hydrolysis in the absence of the central γ rotor.Semantic proximity Read ↗

ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis.Semantic proximity Read ↗

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

The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase.Semantic proximity Read ↗

The depletion of F₁ subunit ε in yeast leads to an uncoupled respiratory phenotype that is rescued by mutations in the proton-translocating subunits of F₀.Semantic proximity Read ↗

Inverse regulation of F1-ATPase activity by a mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase.Semantic proximity Read ↗

Structural analysis of the regulatory dithiol-containing domain of the chloroplast ATP synthase gamma subunit.Semantic proximity Read ↗

ATP synthase from a cyanobacterial Synechocystis 6803 mutant containing the regulatory segment of the chloroplast gamma subunit shows thiol modulation.Semantic proximity Read ↗

ATP-driven rotation of the gamma subunit in F(1)-ATPase.Semantic proximity Read ↗

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