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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

17.9K
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...
17.9K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

6.9K
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...
6.9K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

5.2K
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...
5.2K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

19.0K
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...
19.0K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

10.5K
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...
10.5K
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

4.7K
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...
4.7K

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Related Experiment Video

Updated: Apr 11, 2026

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

Published on: January 22, 2019

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[P4-ATP-ase Atp8b1/FIC1: structural properties and (patho)physiological functions].

T V Korneenko, N B Pestov, I A Okkelman

    Bioorganicheskaia Khimiia
    |June 9, 2015
    PubMed
    Summary

    P4-ATPases, including ATP8B1, transport phospholipids to maintain cell membrane asymmetry. Mutations in ATP8B1 cause serious hereditary diseases like Byler disease, impacting liver and hearing.

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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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    Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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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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    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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    Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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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
    • Cell Biology
    • Genetics

    Context:

    • P4-ATPases are crucial for phospholipid transport across cell membranes.
    • ATP8B1 is a key P4-ATPase isoform implicated in various inherited disorders.
    • Tissue-specific expression and regulatory pathways influence P4-ATPase function.

    Purpose:

    • To elucidate the physiological role of ATP8B1 (FIC1) in phospholipid transport.
    • To understand the molecular basis of pathologies arising from ATP8B1 dysfunction.
    • To explore potential therapeutic targets for ATP8B1-related diseases.

    Summary:

    • ATP8B1 facilitates the translocation of phospholipids like phosphatidylserine and cardiolipin from the outer to the inner plasma membrane leaflet.
    • Loss of ATP8B1 activity disrupts membrane asymmetry, leading to hair cell death in the inner ear and liver cirrhosis due to impaired bile acid transport.
    • ATP8B1 deficiency may also increase susceptibility to bacterial pneumonia.

    Impact:

    • Defines the critical role of ATP8B1 in maintaining cellular homeostasis and preventing inherited diseases.
    • Highlights the connection between membrane asymmetry, phospholipid transport, and severe pathologies.
    • Opens avenues for research into novel therapeutic strategies for cholestasis, hearing loss, and other ATP8B1-related conditions.