Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

Rasmus Kock Flygaard; Alexander Mühleip; Victor Tobiasson; Alexey Amunts

doi:10.1038/s41467-020-18993-6

Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

Rasmus Kock Flygaard, Alexander Mühleip, Victor Tobiasson, Alexey Amunts^*

^*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

39 Citations (Scopus)

Abstract

Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF₁. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.

Original language	English
Article number	5342
Journal	Nature Communications
Volume	11
ISSN	2041-1723
DOIs	https://doi.org/10.1038/s41467-020-18993-6
Publication status	Published - Oct 2020
Externally published	Yes

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title = "Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization",

abstract = "Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 {\AA} resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.",

author = "Flygaard, \{Rasmus Kock\} and Alexander M{\"u}hleip and Victor Tobiasson and Alexey Amunts",

year = "2020",

month = oct,

doi = "10.1038/s41467-020-18993-6",

language = "English",

volume = "11",

journal = "Nature Communications",

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Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization. / Flygaard, Rasmus Kock; Mühleip, Alexander; Tobiasson, Victor et al.
In: Nature Communications, Vol. 11, 5342, 10.2020.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

AU - Flygaard, Rasmus Kock

AU - Mühleip, Alexander

AU - Tobiasson, Victor

AU - Amunts, Alexey

PY - 2020/10

Y1 - 2020/10

N2 - Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.

AB - Mitochondrial ATP synthases form functional homodimers to induce cristae curvature that is a universal property of mitochondria. To expand on the understanding of this fundamental phenomenon, we characterized the unique type III mitochondrial ATP synthase in its dimeric and tetrameric form. The cryo-EM structure of a ciliate ATP synthase dimer reveals an unusual U-shaped assembly of 81 proteins, including a substoichiometrically bound ATPTT2, 40 lipids, and co-factors NAD and CoQ. A single copy of subunit ATPTT2 functions as a membrane anchor for the dimeric inhibitor IF1. Type III specific linker proteins stably tie the ATP synthase monomers in parallel to each other. The intricate dimer architecture is scaffolded by an extended subunit-a that provides a template for both intra- and inter-dimer interactions. The latter results in the formation of tetramer assemblies, the membrane part of which we determined to 3.1 Å resolution. The structure of the type III ATP synthase tetramer and its associated lipids suggests that it is the intact unit propagating the membrane curvature.

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U2 - 10.1038/s41467-020-18993-6

DO - 10.1038/s41467-020-18993-6

M3 - Journal article

C2 - 33093501

AN - SCOPUS:85093917933

SN - 2041-1723

VL - 11

JO - Nature Communications

JF - Nature Communications

M1 - 5342

ER -

Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization

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