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Related Concept Videos

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

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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

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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.
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ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
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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.
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Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.

Yiying Li1, Jie Zhu1, Zhiyin Zhang1

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA, USA.

Nature Chemical Biology
|January 13, 2025
PubMed
Summary
This summary is machine-generated.

Researchers engineered the FtsH enzyme into self-assembling helical nanotubes. These adenosine 5'-triphosphate (ATP)-dependent structures mimic natural cytoskeletal assemblies, using chemical energy for transient formation and degradation.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Molecular Biology

Background:

  • Nucleoside triphosphate (NTP)-dependent protein assemblies like microtubules and actin filaments are crucial in cellular processes and inspire synthetic molecular machines.
  • The functional sophistication of natural systems remains a challenge for artificial design.

Purpose of the Study:

  • To engineer an adenosine 5 -triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system.
  • To alter the structural and functional utilization of chemical energy in an artificial system.

Main Methods:

  • Engineering the FtsH (filamentous temperature-sensitive protease H) hexameric ATPase.
  • Investigating the self-assembly into one-dimensional helical nanotubes.
  • Analyzing ATP hydrolysis and assembly dynamics in the presence of external ATPases.

Main Results:

  • FtsH was successfully engineered into helical nanotubes.
  • These nanotubes are dissipative systems requiring constant ATP input for integrity and degrading over time.
  • Unlike natural systems, ATP hydrolysis is catalyzed by free protomers, and nanotubes conserve ATP, leading to tunable lifetimes.

Conclusions:

  • Engineered FtsH nanotubes represent a novel class of dissipative self-assembling systems.
  • This work demonstrates a new paradigm for utilizing chemical energy in artificial molecular assemblies.
  • The ability to tune assembly lifetimes offers potential for controlled nanomaterial applications.