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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
ATP Synthase: Structure01:18

ATP Synthase: Structure

ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Chemiosmosis01:32

Chemiosmosis

Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
Electron Transport Chain
The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons reduce...

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Related Experiment Video

Updated: Jul 11, 2026

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
08:37

Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Proton paths in the sarcoplasmic reticulum Ca(2+) -ATPase.

Eeva-Liisa Karjalainen1, Karin Hauser, Andreas Barth

  • 1Department of Biochemistry and Biophysics, Stockholm University, Arrhenius Laboratories for Natural Sciences, Svante Arrhenius väg 12, SE-106 91, Stockholm, Sweden.

Biochimica Et Biophysica Acta
|October 2, 2007
PubMed
Summary

The sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) uses separate pathways for calcium and protons. This allows for rapid neutralization of binding sites, improving P-type ATPase function.

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Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart
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Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart

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Last Updated: Jul 11, 2026

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Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle

Published on: March 21, 2025

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
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Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart
09:26

Optical Mapping of Intra-Sarcoplasmic Reticulum Ca2+ and Transmembrane Potential in the Langendorff-perfused Rabbit Heart

Published on: September 10, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The sarcoplasmic reticulum Ca(2+)-ATPase (SERCA1a) is crucial for muscle contraction by pumping calcium ions.
  • Understanding ion transport mechanisms is key to cellular function.

Purpose of the Study:

  • To elucidate the proton pathways in SERCA1a during different functional states.
  • To investigate the structural basis for ion selectivity and transport.

Main Methods:

  • Analysis of crystal structures of SERCA1a.
  • Computational modeling incorporating water molecules to identify ion pathways.

Main Results:

  • Proposed distinct proton pathways in both Ca(2+)-bound (E1) and Ca(2+)-free (E2) states.
  • Identified a proton pathway involving transmembrane helices M5-M8 in the E2 state, distinct from Ca(2+) dissociation routes.
  • Suggested a dual role for a Ca(2+) entry path as a proton pathway in the E1 state.

Conclusions:

  • Separate proton and calcium pathways facilitate rapid neutralization of cation binding sites.
  • This mechanism enhances the efficiency of P-type ATPases by enabling transient protonation and selective ion transport.