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

Critical roles of interdomain interactions for modulatory ATP binding to sarcoplasmic reticulum Ca2+-ATPase.

The Journal of biological chemistry - 17 Oct 2014

Clausen Johannes D, Holdensen Anne Nyholm, Andersen Jens Peter

Abstract excerpt

ATP has dual roles in the reaction cycle of sarcoplasmic reticulum Ca(2+)-ATPase. Upon binding to the Ca2E1 state, ATP phosphorylates the enzyme, and by binding to other conformational states in a non-phosphorylating modulatory mode ATP stimulates the dephosphorylation and other partial reaction steps of the cycle, thereby ensuring a high rate of Ca(2+) transport under physiological conditions. The present study...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Biological Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium

Share to Crystallography, X-Ray

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Rabbits

Share to Sarcoplasmic Reticulum Calcium-Transporting ATPases

Source

Open in PubMed Open full text

Identifiers

PMID: 25193668
DOI: 10.1074/jbc.M114.571687
PMCID: PMC4200266

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical roles of interdomain interactions for modulatory ATP binding to sarcoplasmic reticulum Ca2+-ATPase.PMID 25193668Read ↗

Modulatory ATP binding affinity in intermediate states of E2P dephosphorylation of sarcoplasmic reticulum Ca2+-ATPase.Semantic proximity Read ↗

Localization of a K+ -binding site involved in dephosphorylation of the sarcoplasmic reticulum Ca2+ -ATPase.Semantic proximity Read ↗

Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca2+-ATPase.Semantic proximity Read ↗

[Mechanism of ca(2+) pump as revealed by mutations, development of stable analogs of phosphorylated intermediates, and their structural analyses].Semantic proximity Read ↗

Cooperative setting for long-range linkage of Ca(2+) binding and ATP synthesis in the Ca(2+) ATPase.Semantic proximity Read ↗

The SERCA residue Glu340 mediates interdomain communication that guides Ca2+ transport.Semantic proximity Read ↗

Crystal structure of D351A and P312A mutant forms of the mammalian sarcoplasmic reticulum Ca(2+) -ATPase reveals key events in phosphorylation and Ca(2+) release.Semantic proximity Read ↗

Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2.Semantic proximity Read ↗

Roles of conserved P domain residues and Mg2+ in ATP binding in the ground and Ca2+-activated states of sarcoplasmic reticulum Ca2+-ATPase.Semantic proximity Read ↗

Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum. Mutation Tyr763-->Gly uncouples ATP hydrolysis from Ca2+ transport.Semantic proximity Read ↗

Interhelical hydrogen bonds in transmembrane region are important for function and stability of Ca2+-transporting ATPase.Semantic proximity Read ↗

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

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