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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...
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: Jun 4, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

P-type ATPases.

Michael G Palmgren1, Poul Nissen

  • 1Center for Membrane Pumps in Cells and Disease--PUMPKIN, Danish National Research Foundation, University of Copenhagen, Frederiksberg C, Denmark. palmgren@life.ku.dk

Annual Review of Biophysics
|March 1, 2011
PubMed
Summary

P-type ATPases are essential biological nanomachines that transport ions and lipids. Their atomic structures and mutagenesis reveal detailed insights into their pumping mechanisms across five distinct subfamilies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • P-type ATPases are crucial membrane proteins responsible for transporting cations and lipids.
  • These enzymes feature a single catalytic subunit and undergo significant conformational changes during transport.
  • Understanding their function is vital for cellular homeostasis and various physiological processes.

Purpose of the Study:

  • To elucidate the detailed pumping mechanism of P-type ATPases.
  • To provide insights into the structural basis of their function.
  • To explore the phylogenetic diversity and regulatory differences among P-type ATPase subfamilies.

Main Methods:

  • Determination of atomic structures of P-type ATPases in various functional states.
  • Utilizing extensive mutagenesis studies to probe protein function.

More Related Videos

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

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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

Published on: February 19, 2013

Related Experiment Videos

Last Updated: Jun 4, 2026

Measuring In Vitro ATPase Activity for Enzymatic Characterization
07:38

Measuring In Vitro ATPase Activity for Enzymatic Characterization

Published on: August 23, 2016

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

Measuring Cation Transport by Na,K- and H,K-ATPase in Xenopus Oocytes by Atomic Absorption Spectrophotometry: An Alternative to Radioisotope Assays
12:48

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

Published on: February 19, 2013

  • Phylogenetic analysis to classify P-type ATPases into subfamilies.
  • Main Results:

    • Detailed atomic structures reveal large domain motions during the transport cycle.
    • Mutagenesis data provides functional validation of structural findings.
    • P-type ATPases are classified into five phylogenetically distinct subfamilies (P1-P5).

    Conclusions:

    • The combined structural and mutagenesis data offers a comprehensive understanding of P-type ATPase mechanisms.
    • Subfamilies P1-P5 exhibit variations in transported substrates and regulatory mechanisms.
    • P-type ATPases function as sophisticated biological nanomachines essential for cellular function.