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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...
Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
Primary Active Transport01:29

Primary Active Transport

In contrast to passive transport, active transport involves a substance being moved through membranes in a direction against its concentration or electrochemical gradient. There are two types of active transport: primary active transport and secondary active transport. Primary active transport utilizes chemical energy from ATP to drive protein pumps embedded in the cell membrane. With energy from ATP, the pumps transport ions against their electrochemical gradients—a direction they would not...

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Related Experiment Video

Updated: May 20, 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

Flexible P-type ATPases interacting with the membrane.

Lea Thøgersen1, Poul Nissen

  • 1Centre for Membrane Pumps in Cells and Disease - PUMPKIN, Danish National Research Foundation, DK-8000 Aarhus C, Denmark.

Current Opinion in Structural Biology
|July 4, 2012
PubMed
Summary

P-type ATPases, including cation pumps and lipid flippases, are crucial for maintaining cell membrane integrity and function. Research reveals conserved structural motifs and specific lipid interactions, though transport mechanisms require further investigation.

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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays

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Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
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Area of Science:

  • Membrane protein structure and function
  • Biochemistry and biophysics of ion transport
  • Lipid-protein interactions in biological membranes

Background:

  • P-type ATPases are essential membrane proteins involved in maintaining electrochemical gradients and lipid asymmetry.
  • Specific P-type ATPases like sarcoplasmic reticulum Ca(2+)-ATPase and Na(+),K(+)-ATPase exhibit diverse membrane interactions.
  • The role of protein subunits and membrane lipids in ATPase function is an area of active research.

Purpose of the Study:

  • To elucidate the structural basis of protein:membrane interactions in P-type ATPases.
  • To identify conserved structural motifs and specialized adaptations across different P-type ATPase families.
  • To investigate the molecular determinants of lipid flippase activity in the P4-type ATPase subfamily.

Main Methods:

  • Analysis of crystal structures of P-type ATPases, including a novel heavy-metal transporting ATPase.
  • Examination of protein:membrane interfaces and identification of conserved structural elements.
  • Review of mutational studies to pinpoint key residues for lipid flippase activity.

Main Results:

  • A conserved amphipathic helix at the cytoplasmic membrane surface is identified as a general motif in P-type ATPases.
  • Structural insights reveal adaptations of this motif to different membrane environments.
  • Key residues essential for P4-type ATPase lipid flippase activity have been identified, but the transport pathway remains elusive.

Conclusions:

  • P-type ATPases share a common structural motif for membrane interaction, with specialized variations.
  • Understanding these interactions is crucial for comprehending ion transport and lipid homeostasis.
  • Further research is needed to fully elucidate the transport mechanism and pathway of lipid flippases.