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. Author manuscript; available in PMC: 2025 Sep 5.
Published in final edited form as: Nature. 2023 Aug 23;620(7976):1109–1116. doi: 10.1038/s41586-023-06462-1

Fig. 3: A comparison of s-OPA1 dimers and assembly in the apo and GDP-AlFx bound states.

Fig. 3:

A, Side view of s-OPA1 apo (left) and GDP-AlFx (right) helical structures with a dimer of s-OPA1 colored by domain (see Fig. 1). Models below highlighting the transition from the apo to the GDP-AlFx states, a shift to tighter stalk and paddle interfaces, and a 25–27° swing through hinge-1 of the GTPase and BSE domains. Helices are labeled as in the sequence alignment in Supplementary Fig. 2. B, GTPase dimer formation from apo (left) to GDP-AlFx states (right, interface-5). Membrane location shown in gray. Top left corner, orientation of models shown in cryoEM maps. C, Top, s-OPA1 apo helical structure with a dimer of s-OPA1 colored by domain. Bottom, minimal paddle domain insertion in the membrane. D, Top, s-OPA1 GDP-AlFx helical structure with a dimer of s-OPA1 colored by domain. Bottom, model revealing a deeper paddle domain insertion into the membrane. (c-d) Insets show the membrane-inserting loop that contains Pα2, the membrane-inserting Pα6, and a closer membrane contact for Pα1 and Pα5.