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

Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures.

Nature - 31 Jan 2013

Arai Satoshi, Saijo Shinya, Suzuki Kano, Mizutani Kenji, Kakinuma Yoshimi, Ishizuka-Katsura Yoshiko, Ohsawa Noboru, Terada Takaho, Shirouzu Mikako, Yokoyama Shigeyuki, Iwata So, Yamato Ichiro, Murata Takeshi

Abstract excerpt

In various cellular membrane systems, vacuolar ATPases (V-ATPases) function as proton pumps, which are involved in many processes such as bone resorption and cancer metastasis, and these membrane proteins represent attractive drug targets for osteoporosis and cancer. The hydrophilic V(1) portion is known as a rotary motor, in which a central axis DF complex rotates inside a hexagonally arranged catalytic A(3)B(3)...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Crystallization

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

Share to Enterococcus

Share to Nucleotides

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Rotation

Share to Vacuolar Proton-Translocating ATPases

Source

Identifiers

PMID: 23334411
DOI: 10.1038/nature11778

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

Rotation mechanism of Enterococcus hirae V1-ATPase based on asymmetric crystal structures.PMID 23334411Read ↗

Metastable asymmetrical structure of a shaftless V1 motor.Semantic proximity Read ↗

The F subunit of Thermus thermophilus V1-ATPase promotes ATPase activity but is not necessary for rotation.Semantic proximity Read ↗

A Superfamily of ATPases with Diverse Functions Containing Either Classical or Deviant ATP-binding MotifSemantic proximity Read ↗

ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilus.Semantic proximity Read ↗

The six steps of the complete F1-ATPase rotary catalytic cycle.Semantic proximity Read ↗

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

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

Molecular mechanism of ATP hydrolysis in F1-ATPase revealed by molecular simulations and single-molecule observations.Semantic proximity Read ↗

Comparison between single-molecule and X-ray crystallography data on yeast F1-ATPase.Semantic proximity Read ↗

An Arginine Finger Regulates the Sequential Action of Asymmetrical Hexameric ATPase in the Double-Stranded DNA Translocation Motor.Semantic proximity Read ↗

Foot-and-mouth disease virus 2C is a hexameric AAA+ protein with a coordinated ATP hydrolysis mechanism.Semantic proximity Read ↗

Structural dynamics of AAA+ ATPase Drg1 and mechanism of benzo-diazaborine inhibitionSemantic proximity Read ↗

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