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ATP Synthase

Connect a proton gradient, a rotating molecular motor and ATP production.

Experimental E. coli ATP synthase with a coral c-ring and central rotor, grey and violet catalytic head, grey peripheral stator and gold resolved ligands.
Structural reference

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Quick reference

Stored energy across a membrane

A proton electrochemical gradient has both a concentration component and an electrical component. It can drive protons through the membrane portion of ATP synthase.

Rotation changes binding sites

The rotor couples proton movement to changes in the catalytic head. During synthesis, binding sites bind ADP and phosphate, form ATP and release it. The model steps separate these coupled events for clarity.

A leak bypasses the motor

Proton flow through other routes can dissipate the gradient without driving ATP synthesis. The effect depends on the system maintaining the gradient. This model uses qualitative states, not measured synthesis rates, and leaves reverse operation out of scope.

Check your understanding Optional

A proton leak increases while the system supplies the same input. Why may ATP production decrease?

Choose an answer

At the bench

Explore protein structure and function after seeing how a molecular assembly couples movement to chemistry.

Open Protein
Sources and model notes

Structure-based views of resolved experimental coordinates. Cutaways, category colours, camera choices and guided highlights are authored for teaching. Coordinates remain fixed; highlights are not experimental trajectories or simulation outputs.

RCSB PDB · ATP synthase (opens a new tab)

Structural states and coupling between the two motors.

RCSB PDB · E. coli ATP synthase 6OQR (opens a new tab)

Experimental bacterial assembly; the model is an authored schematic.