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

ATP-driven rotation of the gamma subunit in F(1)-ATPase.

FEBS letters - 13 Oct 2000

Weber J, Nadanaciva S, Senior A E

Abstract excerpt

We present a mechanism for F(1)-ATPase in which hydrolysis of MgATP in the high-affinity catalytic site at the alpha/beta interface drives rotation of the gamma subunit via conformational changes in the alpha subunit. During hydrolysis, transition state formation and separation of P(i) from MgADP causes movement of portions of alpha, transmitted via two Arg residues which are hydrogen-bonded to the...

Read the complete abstract on PubMed

Topics

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

Share to Protein Subunits
Share to Adenosine Triphosphate
Share to Catalytic Domain

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

Share to Hydrolysis

Share to Models, Biological

Share to Mutation

Share to Protein Conformation

Share to Proton-Translocating ATPases

Source

Identifiers

PMID: 11033345
DOI: 10.1016/s0014-5793(00)02071-8

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

ATP-driven rotation of the gamma subunit in F(1)-ATPase.PMID 11033345Read ↗

Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation.Semantic proximity Read ↗

A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis.Semantic proximity Read ↗

Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthase.Semantic proximity Read ↗

Hydrogen bonds between the alpha and beta subunits of the F1-ATPase allow communication between the catalytic site and the interface of the beta catch loop and the gamma subunit.Semantic proximity Read ↗

Met23Lys mutation in subunit gamma of F(O)F(1)-ATP synthase from Rhodobacter capsulatus impairs the activation of ATP hydrolysis by protonmotive force.Semantic proximity Read ↗

Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site.Semantic proximity Read ↗

Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation.Semantic proximity Read ↗

Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation.Semantic proximity Read ↗

Stepwise propagation of the ATP-induced conformational change of the F1-ATPase beta subunit revealed by NMR.Semantic proximity Read ↗

Role of the DELSEED loop in torque transmission of F1-ATPase.Semantic proximity Read ↗

Role of α/β interface in F1 ATPase rotational catalysis probed by inhibitors and mutations.Semantic proximity Read ↗

A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase.Semantic proximity Read ↗

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