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6J54

Cryo-EM structure of the mammalian E-state ATP synthase FO section

Summary for 6J54
Entry DOI10.2210/pdb6j54/pdb
EMDB information0668
DescriptorATP synthase peripheral stalk-membrane subunit b, Mitochondrial H+ transporting ATP synthase subunit c isoform 1, ATP synthase membrane subunit 6.8PL, ... (11 entities in total)
Functional Keywordsmembrane protein
Biological sourceSus scrofa (Pig)
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Total number of polymer chains18
Total formula weight132628.78
Authors
Gu, J.,Zhang, L.,Yi, J.,Yang, M. (deposition date: 2019-01-10, release date: 2019-06-26, Last modification date: 2024-03-27)
Primary citationGu, J.,Zhang, L.,Zong, S.,Guo, R.,Liu, T.,Yi, J.,Wang, P.,Zhuo, W.,Yang, M.
Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1.
Science, 364:1068-1075, 2019
Cited by
PubMed Abstract: 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.
PubMed: 31197009
DOI: 10.1126/science.aaw4852
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.94 Å)
Structure validation

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