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ATP Synthase: Structure

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...

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Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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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 ATP...

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Related Experiment Video

Updated: May 14, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Intersubunit coordination and cooperativity in ring-shaped NTPases.

Ryota Iino¹, Hiroyuki Noji

¹Department of Applied Chemistry, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

Current Opinion in Structural Biology

|February 12, 2013

Summary

Ring-shaped nucleoside triphosphatases (ring NTPases) are molecular machines. High-speed atomic force microscopy offers new insights into their rotary catalysis mechanism.

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Ring-shaped nucleoside triphosphatases (ring NTPases) are essential molecular machines.
These enzymes utilize NTP hydrolysis for cellular functions, involving substrate translocation or subunit rotation.
Understanding subunit coordination and cooperativity within these oligomeric rings is key to elucidating their mechanism.

Purpose of the Study:

To discuss proposed models for ring NTPase operation, including stochastic, concerted, and rotary catalysis.
To introduce high-speed atomic force microscopy (HS-AFM) as a tool for verifying these models.
To present a case study of rotary catalysis in the F1-adenosine triphosphatase stator ring using HS-AFM.

Main Methods:

X-ray crystallographic structural analysis.
Optical microscopic single-molecule studies.
High-speed atomic force microscopy (HS-AFM).

Main Results:

Distinct mechanistic models (stochastic, concerted, rotary catalysis) have been proposed based on structural and single-molecule data.
HS-AFM provides high-resolution dynamic information crucial for model verification.
Recent HS-AFM studies exemplify the rotary catalysis mechanism of the F1-adenosine triphosphatase stator ring.

Conclusions:

HS-AFM is a powerful technique for investigating the dynamic mechanisms of ring NTPases.
The study supports the rotary catalysis model for F1-adenosine triphosphatase.
Further application of HS-AFM will advance our understanding of these vital molecular machines.