9JC1

Engineering of ATP synthase

Summary for 9JC1

• Entry DOI: 10.2210/pdb9jc1/pdb
• EMDB information: 61339
• Descriptor: ATP synthase subunit beta, ATP synthase gamma chain, ATP synthase epsilon chain, ... (8 entities in total)
• Functional Keywords: molecular motor, atp synthase, membrane protein
• Biological source: Bacillus sp. PS3; More
• Total number of polymer chains: 14
• Total formula weight: 505741.21

Authors

Hamaguchi-Suzuki, N.,Ueno, H.,Yasuda, K.,Marui, R.,Adachi, N.,Senda, T.,Noji, H.,Murata, T. (deposition date: 2024-08-28, release date: 2025-07-09, Last modification date: 2025-07-16)

Primary citation

Ueno, H.,Yasuda, K.,Hamaguchi-Suzuki, N.,Marui, R.,Adachi, N.,Senda, T.,Murata, T.,Noji, H.
Engineering of ATP synthase for enhancement of proton-to-ATP ratio.
Nat Commun, 16:5410-5410, 2025

PubMed Abstract: FF-ATP synthase (FF) interconverts the energy of the proton motive force (pmf) and that of ATP through the mechanical rotation. The H/ATP ratio, one of the most crucial parameters in bioenergetics, varies among species due to differences in the number of H-binding c-subunits, resulting in H/ATP ratios ranging from 2.7 to 5. In this study, we seek to significantly enhance the H/ATP ratio by employing an alternative approach that differs from that of nature. We engineer FF to form multiple peripheral stalks, each bound to a proton-conducting a-subunit. The engineered FF exhibits an H/ATP ratio of 5.8, surpassing the highest ratios found in naturally occurring FFs, enabling ATP synthesis under low pmf conditions where wild-type enzymes cannot synthesize ATP. Structural analysis reveals that the engineered FF forms up to three peripheral stalks and a-subunits. This study not only provides valuable insights into the H-transport mechanism of FF but also opens up possibilities for engineering the foundation of cellular bioenergetics.

PubMed: 40610443
DOI: 10.1038/s41467-025-61227-w

Experimental method

ELECTRON MICROSCOPY (2.79 Å)