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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

4.5K
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...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

11.9K
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...
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ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

3.6K
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...
3.6K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.0K
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...
8.0K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

13.9K
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...
13.9K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

3.2K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Related Experiment Video

Updated: Jun 8, 2025

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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The structure and function of P5A-ATPases.

Ping Li1, Viktoria Bågenholm2, Per Hägglund2

  • 1Department of Experimental Medical Science, Lund University, Sölvegatan 19, SE-221 84, Lund, Sweden. ping.li@med.lu.se.

Nature Communications
|November 6, 2024
PubMed
Summary
This summary is machine-generated.

P5A-ATPases are crucial for protein quality control in the endoplasmic reticulum. This study reveals their transport mechanisms, showing how they bind and move protein cargo across membranes, potentially aiding in protein removal or insertion.

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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Related Experiment Videos

Last Updated: Jun 8, 2025

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 In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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Area of Science:

  • Structural Biology
  • Molecular Cell Biology
  • Biochemistry

Background:

  • Endoplasmic reticulum (ER) membrane-resident P5A-ATPases play a broad role in protein biogenesis and quality control.
  • The precise molecular function of P5A-ATPases remains incompletely understood.
  • Understanding these ATPases is critical for deciphering cellular protein management pathways.

Purpose of the Study:

  • To elucidate the molecular mechanism of P5A-ATPases by determining their structural dynamics.
  • To visualize the transport cycle of a P5A-ATPase, CtSpf1, at high resolution.
  • To identify potential protein cargo and the role of specific structural domains.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to capture multiple structural states.
  • Structures were determined for various intermediates of the CtSpf1 ATPase catalytic cycle (E1 to E2 states).
  • Analysis focused on conformational changes, substrate binding sites, and domain movements.

Main Results:

  • Cryo-EM structures revealed distinct conformations of CtSpf1 throughout its catalytic cycle.
  • In E2P and E2.Pi states, a transmembrane cleft was observed, binding a polypeptide cargo.
  • The E1 state structure showed a cytosol-facing cavity occluded by a 'Plug-domain', which is displaced in later states.

Conclusions:

  • P5A-ATPases likely bind a diverse range of protein cargoes.
  • The observed structural features suggest a role in removing transmembrane helices, with insertion or secretion as possibilities.
  • The Plug-domain appears to play a crucial mechanistic role in the ATPase function and substrate translocation.