Studying atp synthesis in situ


Play all audios:

Access through your institution Buy or subscribe Mitochondria have a crucial role in replenishing ATP, the molecule used to provide cellular energy. This is achieved by tightly coupling the


movement of protons (H+) across the inner mitochondrial membrane to power the rotary action of ATP synthase in the final step of oxidative phosphorylation. Folds of the inner mitochondrial


membrane called cristae provide a large, ion-impermeable surface area studded with respiratory enzymes including ATP synthase dimers. Structures of isolated ATP synthases have previously


been determined, and by reconstituting into liposomes were observed to spontaneously form dimer rows that curve the liposomal membrane; however, the structure of ATP synthase has not been


determined in its natural environment, which preserves the electrochemical proton gradient. Now, using cryo-electron tomography (cryo-ET), Dietrich et al. have determined the structure of


the mitochondrial ATP synthase within the unicellular alga _Polytomella_, which was flash-frozen under active growth conditions. The team observed an arrangement of parallel rows of ATP


synthase dimers that twist around the cristae ridges with a left-handed helical geometry. The ATP synthase dimer rows define the shape of the cristae. This is a preview of subscription


content, access via your institution ACCESS OPTIONS Access through your institution Access Nature and 54 other Nature Portfolio journals Get Nature+, our best-value online-access


subscription $29.99 / 30 days cancel any time Learn more Subscribe to this journal Receive 12 print issues and online access $259.00 per year only $21.58 per issue Learn more Buy this


article * Purchase on SpringerLink * Instant access to full article PDF Buy now Prices may be subject to local taxes which are calculated during checkout ADDITIONAL ACCESS OPTIONS: * Log in


* Learn about institutional subscriptions * Read our FAQs * Contact customer support AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Nature Communications https://www.nature.com/ncomms/


Benjamin McIlwain Authors * Benjamin McIlwain View author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Benjamin McIlwain.


RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE McIlwain, B. Studying ATP synthesis in situ. _Nat Chem Biol_ 20, 1387 (2024).


https://doi.org/10.1038/s41589-024-01768-1 Download citation * Published: 22 October 2024 * Issue Date: November 2024 * DOI: https://doi.org/10.1038/s41589-024-01768-1 SHARE THIS ARTICLE


Anyone you share the following link with will be able to read this content: Get shareable link Sorry, a shareable link is not currently available for this article. Copy to clipboard Provided


by the Springer Nature SharedIt content-sharing initiative