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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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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...
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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.
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 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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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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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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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.0K
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...
8.0K
Energy to Drive Translocation01:37

Energy to Drive Translocation

2.0K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Torque generation of Enterococcus hirae V-ATPase.

Hiroshi Ueno1, Yoshihiro Minagawa2, Mayu Hara2

  • 1From the Department of Physics, Faculty of Science and Engineering, Chuo University, Tokyo 112-8551, Japan.

The Journal of Biological Chemistry
|September 27, 2014
PubMed
Summary

The V-ATPase (V(o)V1) enzyme converts ATP energy into ion force through mechanical rotation. This study reveals rotor-stator interactions in Enterococcus hirae V-ATPase stabilize rotation, generating higher torque but indicating lower energy efficiency.

Keywords:
BioenergeticsMembrane ProteinMolecular MotorSingle-molecule BiophysicsV-ATPaseVacuolar ATPase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzyme Kinetics

Background:

  • V-ATPase (V(o)V1) is a rotary motor enzyme that couples ATP hydrolysis to ion transport.
  • Efficient energy conversion relies on precise rotor-stator interactions within the V(o)V1 complex.
  • Understanding these interactions is crucial for elucidating enzyme mechanism and efficiency.

Purpose of the Study:

  • To characterize the mechanical properties and torque generation of Enterococcus hirae V-ATPase (EhV(o)V1).
  • To compare the functional equivalence and rotational behavior of recombinant EhV(o)V1 with native V(o)V1.
  • To investigate the role of rotor-stator interactions in torque generation and energy conversion efficiency.

Main Methods:

  • Development of an Escherichia coli expression system for recombinant EhV(o)V1.
  • Establishment of a single-molecule rotation assay to measure torque.
  • Analysis of ATP hydrolysis activity dependence on sodium and ATP concentrations.
  • Characterization of rotational behavior using low and large load probes.

Main Results:

  • Recombinant and native EhV(o)V1 showed similar ATP hydrolysis kinetics.
  • EhV(o)V1 exhibited unique rotational states and lacked distinct 120° pauses observed in EhV1.
  • EhV(o)V1 generated nearly double the continuous rotation torque compared to EhV1, despite comparable stepping torque.
  • Rotor-stator interactions in EhV(o)V1, stabilized by peripheral stalks, limit V1 moiety rotation.

Conclusions:

  • Rotor-stator interactions in the V(o) moiety and/or sodium ion transport limit rotation driven by the V1 moiety.
  • Stabilized rotor-stator interactions in EhV(o)V1 enhance torque generation compared to isolated V1.
  • The overall energy conversion efficiency of EhV(o)V1 is relatively low compared to other rotary ATPases.