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

Role of the DELSEED loop in torque transmission of F1-ATPase.

Biophysical journal - 5 Sept 2012

Tanigawara Mizue, Tabata Kazuhito V, Ito Yuko, Ito Jotaro, Watanabe Rikiya, Ueno Hiroshi, Ikeguchi Mitsunori, Noji Hiroyuki

Abstract excerpt

F(1)-ATPase is an ATP-driven rotary motor that generates torque at the interface between the catalytic β-subunits and the rotor γ-subunit. The β-subunit inwardly rotates the C-terminal domain upon nucleotide binding/dissociation; hence, the region of the C-terminal domain that is in direct contact with γ-termed the DELSEED loop-is thought to play a critical role in torque transmission. We substituted all the...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Bacillus

Share to Kinetics

Share to Molecular Dynamics Simulation

Share to Protein Structure, Tertiary

Share to Proton-Translocating ATPases

Share to Rotation

Source

Open in PubMed Open full text

Identifiers

PMID: 23009846
DOI: 10.1016/j.bpj.2012.06.054
PMCID: PMC3433597

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the DELSEED loop in torque transmission of F1-ATPase.PMID 23009846Read ↗

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 ↗

The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit.Semantic proximity Read ↗

None of the rotor residues of F1-ATPase are essential for torque generation.Semantic proximity Read ↗

The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.Semantic proximity Read ↗

Dissecting the role of the γ-subunit in the rotary-chemical coupling and torque generation of F1-ATPase.Semantic proximity Read ↗

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

Axle-less F1-ATPase rotates in the correct direction.Semantic proximity Read ↗

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

Torque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.Semantic proximity Read ↗

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

Mutational analysis of F1F0 ATPase: catalysis and energy coupling.Semantic proximity Read ↗

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