6J54
Cryo-EM structure of the mammalian E-state ATP synthase FO section
Summary for 6J54
Entry DOI | 10.2210/pdb6j54/pdb |
EMDB information | 0668 |
Descriptor | ATP 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 Keywords | membrane protein |
Biological source | Sus scrofa (Pig) More |
Total number of polymer chains | 18 |
Total formula weight | 132628.78 |
Authors | |
Primary citation | Gu, 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: 31197009DOI: 10.1126/science.aaw4852 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.94 Å) |
Structure validation
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