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

Second transmembrane helix (M2) and long range coupling in Ca²⁺-ATPase.

The Journal of biological chemistry - 7 Nov 2014

Daiho Takashi, Yamasaki Kazuo, Danko Stefania, Suzuki Hiroshi

Abstract excerpt

The actuator (A) domain of sarco(endo)plasmic reticulum Ca(2+)-ATPase not only plays a catalytic role but also undergoes large rotational movements that influence the distant transport sites through connections with transmembrane helices M1 and M2. Here we explore the importance of long helix M2 and its junction with the A domain by disrupting the helix structure and elongating with insertions of five glycine...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Transporting ATPases
Share to Chlorocebus aethiops
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to Glycine

Share to Microsomes

Share to Protein Structure, Secondary

Share to Sarcoplasmic Reticulum

Source

Open in PubMed Open full text

Identifiers

PMID: 25246522
DOI: 10.1074/jbc.M114.584086
PMCID: PMC4223325

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

Second transmembrane helix (M2) and long range coupling in Ca²⁺-ATPase.PMID 25246522Read ↗

Assembly of a Tyr122 Hydrophobic Cluster in Sarcoplasmic Reticulum Ca2+-ATPase Synchronizes Ca2+ Affinity Reduction and Release with Phosphoenzyme Isomerization.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 ↗

Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+ -releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+ -ATPase.Semantic proximity Read ↗

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

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

Structural basis for alpha1 versus alpha2 isoform-distinct behavior of the Na,K-ATPase.Semantic proximity Read ↗

Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses.Semantic proximity Read ↗

Val200 residue in Lys189-Lys205 outermost loop on the A domain of sarcoplasmic reticulum Ca2+-ATPase is critical for rapid processing of phosphoenzyme intermediate after loss of ADP sensitivity.Semantic proximity Read ↗

Modulatory ATP binding affinity in intermediate states of E2P dephosphorylation 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 ↗

A Darier disease mutation relieves kinetic constraints imposed by the tail of sarco(endo)plasmic reticulum Ca2+-ATPase 2b.Semantic proximity Read ↗

A conformation-specific interhelical salt bridge in the K+ binding site of gastric H,K-ATPase.Semantic proximity Read ↗

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