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ATP Synthase: Structure01:18

ATP Synthase: Structure

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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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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...
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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ATP Driven Pumps II: P-type Pumps01:34

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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.
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The ADP/ATP Carrier Protein01:42

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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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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans.

Soumya Mohanty1, Chacko Jobichen1, Vishnu Priyanka Reddy Chichili1

  • 1Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.

The Journal of Biological Chemistry
|September 16, 2015
PubMed
Summary
This summary is machine-generated.

This study reveals that the archaeal ATP synthase from Nanoarcheaum equitans, despite having a core structure, may not function as a typical ATP synthase. Its unique regulatory subunit and rigid conformation suggest a potentially rudimentary energy mechanism.

Keywords:
ATP synthaseNanoarchaeum equitansarchaeacatalytic corecrystal structureevolutionprotein complex

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • ATP synthesis is vital for life, with well-studied eukaryotic and prokaryotic ATP synthases.
  • Archaeal ATP synthases, particularly in hyperthermophiles like Nanoarcheaum equitans, are less understood.
  • N. equitans, an archaeal parasite, may rely on its host for energy, suggesting a simplified ATP synthase.

Purpose of the Study:

  • To investigate the structure and function of the ATP synthase regulatory subunit (NeqB) from N. equitans.
  • To characterize the NeqAB complex, including its nucleotide-binding properties and conformational dynamics.
  • To determine if the N. equitans ATP synthase operates as a functional enzyme.

Main Methods:

  • X-ray crystallography was used to determine the structures of NeqB, apo-NeqAB, and NeqAB-nucleotide complexes.
  • Biophysical studies were conducted to analyze nucleotide binding and conformational changes.
  • Comparative analysis with homologous ATP synthases was performed.

Main Results:

  • The crystal structures of NeqB, apo-NeqAB, and NeqAB with ADP and AMP-PNP were determined.
  • NeqB is shorter at the C terminus but retains binding capability with NeqA.
  • The NeqAB complex exhibits a rigid, closed conformation, independent of nucleotide binding, unlike other ATP synthases.

Conclusions:

  • The N. equitans ATP synthase complex, despite possessing a core A3B3 hexamer, shows structural and conformational properties distinct from functional ATP synthases.
  • The rigid conformation suggests a potential lack of catalytic activity or a significantly altered mechanism of ATP synthesis.
  • This archaeal ATP synthase may represent a rudimentary or non-canonical energy-generating machine.