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Related Concept Videos

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...
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...
The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Related Experiment Video

Updated: May 29, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

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

Published on: September 14, 2014

Mitochondrial ATP synthase: architecture, function and pathology.

An I Jonckheere1, Jan A M Smeitink, Richard J T Rodenburg

  • 1Department of Pediatrics, Nijmegen Center for Mitochondrial Disorders, 656 Laboratory for Genetic, Endocrine, and Metabolic Disorders, Radboud University Nijmegen Medical Center, PO Box 9101, 6500 HB, Nijmegen, The Netherlands.

Journal of Inherited Metabolic Disease
|August 30, 2011
PubMed
Summary
This summary is machine-generated.

Human mitochondrial ATP synthase (Complex V) generates cellular energy. This review details its structure, function, assembly, and links to disease, highlighting areas for future research and therapy.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Respiration

Background:

  • Mitochondrial ATP synthase (Complex V) is crucial for cellular energy production.
  • It comprises F(1) and F(o) domains, utilizing proton gradients to synthesize ATP.
  • Understanding its structure, function, and assembly is vital for cellular health.

Purpose of the Study:

  • To provide a comprehensive review of human mitochondrial ATP synthase (Complex V).
  • To discuss its architecture, function, and assembly processes.
  • To highlight the role of oligomerization, its relation to mitochondrial morphology, and pathologies associated with Complex V deficiency.

Main Methods:

  • Literature review of existing research on mitochondrial ATP synthase.
  • Analysis of structural and functional data.
  • Discussion of pathological findings and therapeutic strategies.

Main Results:

  • Complex V's architecture, function, and assembly are intricate processes.
  • Oligomerization of Complex V influences mitochondrial morphology.
  • Complex V deficiency leads to various pathologies, with ongoing therapeutic developments.

Conclusions:

  • Significant progress has been made in understanding Complex V, but key questions remain regarding subunit structure and the molecular function of its rotary nanomotor.
  • Further research into human Complex V assembly and genetic defects is needed.
  • Elucidating these aspects will advance physiological and pathological studies, guiding future therapeutic interventions for Complex V-related disorders.