Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1

The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase d...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2019-06, Vol.364 (6445), p.1068-1075
Main Authors: Gu, Jinke, Zhang, Laixing, Zong, Shuai, Guo, Runyu, Liu, Tianya, Yi, Jingbo, Wang, Peiyi, Zhuo, Wei, Yang, Maojun
Format: Article
Language:English
Subjects:
Adenosine triphosphate
Animals
ATP
ATP synthase
ATPase Inhibitory Protein
Cellular manufacture
Cryoelectron Microscopy
Dimers
Electron microscopy
Mammalian cells
Mammals
Mitochondria
Mitochondrial Proton-Translocating ATPases - antagonists & inhibitors
Mitochondrial Proton-Translocating ATPases - chemistry
Mitochondrial Proton-Translocating ATPases - isolation & purification
Protein Conformation
Protein Multimerization
Proteins
Proteins - chemistry
Swine
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Summary:The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo-electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.aaw4852