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Related Concept Videos

ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

4.9K
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 Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.3K
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...
8.3K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

3.8K
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...
3.8K
ATP Synthase: Structure01:18

ATP Synthase: Structure

12.7K
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...
12.7K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

14.8K
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...
14.8K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

3.3K
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...
3.3K

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Related Experiment Video

Updated: Jul 28, 2025

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

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Fast-forward on P-type ATPases: recent advances on structure and function.

Charlott Stock1,2, Tomáš Heger1,2, Sara Basse Hansen1,2

  • 1Nordic-EMBL Partnership for Molecular Medicine, Danish Research Institute of Translational Neuroscience - DANDRITE, Aarhus, Denmark.

Biochemical Society Transactions
|June 2, 2023
PubMed
Summary
This summary is machine-generated.

P-type ATPases are vital cellular pumps. Recent cryo-electron microscopy (cryo-EM) studies reveal diverse structures and regulatory mechanisms across P-type ATPase subfamilies, advancing our understanding of these essential proteins.

Keywords:
P-type atpasesactivitycryo-EMregulation

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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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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Related Experiment Videos

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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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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Physiology

Background:

  • P-type ATPases are essential transmembrane proteins found in all organisms.
  • They maintain electrochemical gradients, control membrane lipid asymmetry, and participate in signaling networks.
  • These ATPases share a common topology and follow the Post-Albers transport cycle.

Approach:

  • This review highlights recent advancements in P-type ATPase research, particularly driven by cryo-electron microscopy (cryo-EM).
  • It focuses on the unique features and mechanisms of the five P-type ATPase subfamilies.
  • The review synthesizes findings on structures, functions, and regulatory strategies.

Key Points:

  • Cryo-EM has significantly advanced the understanding of P-type ATPase structures and mechanisms.
  • Specific subfamily features discussed include KdpFABC, heavy metal pumps, Ca2+ pumps, Na,K- and H,K-ATPases, fungal proton pumps, P4-ATPase lipid flippases, and P5 pumps.
  • Many features are conserved or mixed across subfamilies, enabling versatile function and regulation.

Conclusions:

  • P-type ATPases exhibit remarkable diversity in structure and function across their subfamilies.
  • Adaptive strategies and regulatory mechanisms allow these pumps to meet specific cellular and environmental demands.
  • The integration of features across subfamilies underscores their evolutionary adaptability and functional optimization.