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

Role of alphaPhe-291 residue in the phosphate-binding subdomain of catalytic sites of Escherichia coli ATP synthase.

Archives of biochemistry and biophysics - 15 Mar 2008

Brudecki Laura E, Grindstaff Johnny J, Ahmad Zulfiqar

Abstract excerpt

The role of alphaPhe-291 residue in phosphate binding by Escherichia coli F1F0-ATP synthase was examined. X-ray structures of bovine mitochondrial enzyme suggest that this residue resides in close proximity to the conserved betaR246 residue. Herein, we show that mutations alphaF291D and alphaF291E in E. coli reduce the ATPase activity of F1F0 membranes by 350-fold. Yet, significant oxidative phosphorylation...

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 Aluminum
Share to Azides

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

Share to Catalytic Domain

Share to Hydrolysis

Share to Phenylalanine

Share to Phosphates

Share to Tyrosine

Source

Identifiers

PMID: 18242162
DOI: 10.1016/j.abb.2008.01.013

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

Role of alphaPhe-291 residue in the phosphate-binding subdomain of catalytic sites of Escherichia coli ATP synthase.PMID 18242162Read ↗

Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Semantic proximity Read ↗

Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Semantic proximity Read ↗

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.Semantic proximity Read ↗

alpha-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPase.Semantic proximity Read ↗

Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.Semantic proximity Read ↗

Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase.Semantic proximity Read ↗

Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching.Semantic proximity Read ↗

The Escherichia coli F1-ATPase mutant beta Tyr-297-->Cys: functional studies and asymmetry of the enzyme under various nucleotide conditions based on reaction of the introduced Cys with N-ethylmaleimide and 7-chloro-4-nitrobenzofurazan.Semantic proximity Read ↗

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Semantic proximity Read ↗

Suppressor mutations in F1 subunit epsilon recouple ATP-driven H+ translocation in uncoupled Q42E subunit c mutant of Escherichia coli F1F0 ATP synthase.Semantic proximity Read ↗

Identification of substrate contact residues important for the allosteric regulation of phosphofructokinase from Eschericia coli.Semantic proximity Read ↗

The holo-form of the nucleotide binding domain of the KdpFABC complex from Escherichia coli reveals a new binding mode.Semantic proximity Read ↗

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