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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

13.3K
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 Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.4K
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...
15.4K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.7K
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...
8.7K
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

336
The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
336
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

3.5K
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...
3.5K
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

5.9K
Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Related Experiment Video

Updated: Oct 1, 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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ATP synthase FOF1 structure, function, and structure-based drug design.

Alexey V Vlasov1,2, Stepan D Osipov1, Nikolay A Bondarev1

  • 1Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, 141700, Dolgoprudny, Russia.

Cellular and Molecular Life Sciences : CMLS
|March 7, 2022
PubMed
Summary

This review explores F-type ATP synthases, vital molecular machines for cellular energy. Understanding their structure aids in developing new therapies for related disorders.

Keywords:
FOF1 ATP synthaseIntrinsically disordered proteins (IDP)Isopronoid quinonesMembrane proteinsSmall-molecule cofactorsStructure-based drug design

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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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F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes
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F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

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Last Updated: Oct 1, 2025

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes
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F1FO ATPase Vesicle Preparation and Technique for Performing Patch Clamp Recordings of Submitochondrial Vesicle Membranes

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Energetics

Background:

  • ATP synthases (FOF1) are rotary molecular machines essential for cellular energy production, synthesizing adenosine triphosphate (ATP).
  • These enzymes are crucial for maintaining transmembrane potential and are implicated in cell death regulation and mitochondrial permeability transition pore formation.
  • Dysfunction of ATP synthases leads to severe, often fatal, human disorders.

Purpose of the Study:

  • To review the structure-based approach for developing novel therapies targeting FOF1 ATP synthases.
  • To analyze and systematize information on the structural organization of FOF1 across different taxonomic groups.
  • To discuss the potential for designing tools to control cellular bioenergetics.

Main Methods:

  • Systematic review and analysis of existing literature on FOF1 ATP synthase structure.
  • Comparative analysis of structural features across diverse taxonomic representatives of the enzyme family.
  • Literature-based discussion on therapeutic strategies and bioenergetic control tools.

Main Results:

  • Key subunits of ATP synthases are conserved, but structural organization and subunit composition vary significantly across species.
  • FOF1 ATP synthases exhibit diverse structural features inherited from different taxonomic groups.
  • The review consolidates structural information relevant for therapeutic development and bioenergetic control.

Conclusions:

  • A structure-based approach utilizing conserved and diverse FOF1 features can guide the development of targeted therapies.
  • Understanding ATP synthase structure is key to designing novel tools for modulating cellular bioenergetics.
  • This approach holds promise for treating severe disorders linked to ATP synthase dysfunction.