Cryo-EM structures of S-OPA1 reveal its interactions with membrane and changes upon nucleotide binding

Bibliographic Details
Title: Cryo-EM structures of S-OPA1 reveal its interactions with membrane and changes upon nucleotide binding
Authors: Danyang Zhang, Yan Zhang, Jun Ma, Chunmei Zhu, Tongxin Niu, Wenbo Chen, Xiaoyun Pang, Yujia Zhai, Fei Sun
Source: eLife, Vol 9 (2020)
Publisher Information: eLife Sciences Publications Ltd, 2020.
Publication Year: 2020
Collection: LCC:Medicine
LCC:Science
LCC:Biology (General)
Subject Terms: cryo-electron microscopy, conformational change, mitochondrial fusion, membrane tubulation, OPA1, Medicine, Science, Biology (General), QH301-705.5
More Details: Mammalian mitochondrial inner membrane fusion is mediated by optic atrophy 1 (OPA1). 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–coated liposomes in nucleotide-free and GTPγS-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 GTPγS 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2050-084X
Relation: https://elifesciences.org/articles/50294; https://doaj.org/toc/2050-084X
DOI: 10.7554/eLife.50294
Access URL: https://doaj.org/article/eadd3d0efa0f4127a510dff72fab2be0
Accession Number: edsdoj.3d0efa0f4127a510dff72fab2be0
Database: Directory of Open Access Journals
More Details
ISSN:2050084X
DOI:10.7554/eLife.50294
Published in:eLife
Language:English