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

Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.

FEBS letters - 2 Apr 2013

DeLeon-Rangel Jessica, Ishmukhametov Robert R, Jiang Warren, Fillingame Robert H, Vik Steven B

Abstract excerpt

The interaction of the membrane traversing stator subunits a and b of the rotary ATP synthase was probed by substitution of a single Cys into each subunit with subsequent Cu(2+) catalyzed cross-linking. Extensive interaction between the transmembrane (TM) region of one b subunit and TM2 of subunit a was indicated by cross-linking with 6 Cys pairs introduced into these regions. Additional disulfide cross-linking...

Read the complete abstract on PubMed

Topics

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

Share to Cross-Linking Reagents
Share to Cysteine
Share to Disulfides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Immunoblotting

Share to Maleimides

Share to Protein Multimerization

Share to Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 23416299
DOI: 10.1016/j.febslet.2013.02.012
PMCID: PMC3608841

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Interactions between subunits a and b in the rotary ATP synthase as determined by cross-linking.PMID 23416299Read ↗

Characterization of the first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase by surface labeling, cross-linking, and mutagenesis.Semantic proximity Read ↗

Intersubunit crosslinking of the heterotetrameric proton-translocating pyridine nucleotide transhydrogenase of Escherichia coli defines intersubunit contacts between transmembrane helices of the beta subunits.Semantic proximity Read ↗

Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain.Semantic proximity Read ↗

Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex.Semantic proximity Read ↗

Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase.Semantic proximity Read ↗

TM2 but not TM4 of subunit c'' interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking.Semantic proximity Read ↗

Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links.Semantic proximity Read ↗

Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.Semantic proximity Read ↗

Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.Semantic proximity Read ↗

The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling.Semantic proximity Read ↗

Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking.Semantic proximity Read ↗

The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli.Semantic proximity Read ↗

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