ATP synthase is a crucial enzyme in cellular metabolism that synthesizes ATP from ADP and inorganic phosphate, utilizing energy from an electrochemical gradient. Composed of eight subunit types, its structure includes a soluble F1 portion and a membrane-embedded FO portion, with proton movement driving ATP production. This process highlights the role of ATP as the primary energy currency in all living organisms.

1. Molecular Motor-ATP SYNTHASE
By-Lovnish Thakur
ASU2014010100099
3rd SEM, Integrated Biotech

2. Introduction
All living organisms, from bacteria, fungi, spinach and
worms to crocodiles and humans, use ATP for energy
conversion. Originally, the energy comes from the sun.
Plants capture it during photosynthesis and convert it to
chemical energy as ATP. Using this energy, plants
produce carbohydrates, fats and proteins which are
eaten by animals and human beings. In metabolism,
the food is broken down and the energy released is
used to make ATP. Energy is interconverted between
various forms. ATP is an energy currency.

3. ATP
• ATP is the most commonly used "energy
currency" of cells from most organisms. It is
formed from adenosine diphosphate (ADP) and
inorganic phosphate (Pi), and needs energy.
• The overall reaction sequence is: ADP + Pi → ATP,
where ADP and Pi are joined together by ATP
synthase
• ATP synthase utilizes the energy stored in this
electrochemical gradient to drive nucleotide
synthesis.

4. ATP Synthase
ATP synthase—also called FoF1 ATPase is the
universal protein that terminates oxidative
phosphorylation by synthesizing ATP from ADP
and phosphate.
ATP Synthase is one of the most important
enzymes found in the mitochondria of cells

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6. Structure
• ATP synthase is composed of at least 8 subunit
types, whose stochiometry is denoted with
subscripts: (a3, b3, g, d, e, a6, b2, c12), which
combine into two distinct regions.
• The F1 portion is soluble and consists of a
hexamer, a3b3. This hexamer is arranged in an
annulus about a central shaft consisting of the
coiled-coil g subunit.
• The Fo portion consists of three transmembrane
subunits: a6, b2 and c12.

8. Working
ATP synthesis does not require the input of
energy, but the release of the newly
synthesized ATP does require energy.
The movement of protons through the F0
channel causes the γ subunit to rotate which
drives a conformational change in the
structure of the β-subunit resulting in the
binding of substrates (ADP and Pi) and the
release of the product ATP.

9. www.diapedia.org

10. Reference
• www.denstoredanske.dk/Natur_og.../ATPsynt
ase
• thegrantlab.org/resources/handout_motors_
CSUSM_11.pdf
• https://www.rpi.edu/dept/bcbp/molbiochem/
MBWeb/mb1/.../f1fo.htm

11. THANK YOU