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Under physiological conditions, OPA1 undergoes proteolytic processing to form a membrane-anchored long isoform (L-OPA1) and a soluble short isoform (S-OPA1). A combination of L-OPA1 and S-OPA1 is essential for efficient membrane fusion; however, the relevant mechanism is not well understood. In this study, we investigate the cryo-electron microscopic structures of S-OPA1\u2013coated liposomes in nucleotide-free and GTP\u03b3S-bound states. S-OPA1 exhibits a general dynamin-like structure and can assemble onto membranes in a helical array with a dimer building block. We reveal that hydrophobic residues in its extended membrane-binding domain are critical for its tubulation activity. The binding of GTP\u03b3S triggers a conformational change and results in a rearrangement of the helical lattice and tube expansion similar to that of S-Mgm1. These observations indicate that S-OPA1 adopts a dynamin-like power stroke membrane remodeling mechanism during mitochondrial inner membrane fusion.<\/jats:p>","DOI":"10.7554\/elife.50294","type":"journal-article","created":{"date-parts":[[2020,3,31]],"date-time":"2020-03-31T08:03:18Z","timestamp":1585641798000},"source":"Crossref","is-referenced-by-count":69,"title":["Cryo-EM structures of S-OPA1 reveal its interactions with membrane and changes upon nucleotide binding"],"prefix":"10.7554","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7279-9267","authenticated-orcid":true,"given":"Danyang","family":"Zhang","sequence":"first","affiliation":[{"name":"National Key Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China"},{"name":"University of Chinese Academy of Sciences, Beijing, 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