6J5K

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

This is a non-PDB format compatible entry.

Summary for 6J5K

• Entry DOI: 10.2210/pdb6j5k/pdb
• EMDB information: 0667
• Descriptor: ATP synthase F1 subunit alpha, ATP synthase subunit d, mitochondrial, ATP synthase subunit e, ... (22 entities in total)
• Functional Keywords: membrane protein
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 120
• Total formula weight: 2294307.37

Authors

Gu, J.,Zhang, L.,Yi, J.,Yang, M. (deposition date: 2019-01-11, release date: 2019-06-26, Last modification date: 2024-03-27)

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

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

Experimental method

ELECTRON MICROSCOPY (6.2 Å)