8H9L

Human ATP synthase F1 domain, state 3a

This is a non-PDB format compatible entry.

Summary for 8H9L

• Entry DOI: 10.2210/pdb8h9l/pdb
• EMDB information: 34572
• Descriptor: ATP synthase subunit alpha, mitochondrial, ATP synthase subunit beta, mitochondrial, ATP synthase subunit gamma, mitochondrial, ... (8 entities in total)
• Functional Keywords: membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 9
• Total formula weight: 384444.71

Authors

Lai, Y.,Zhang, Y.,Liu, F.,Gao, Y.,Gong, H.,Rao, Z. (deposition date: 2022-10-25, release date: 2023-05-31, Last modification date: 2024-07-03)

Primary citation

Lai, Y.,Zhang, Y.,Zhou, S.,Xu, J.,Du, Z.,Feng, Z.,Yu, L.,Zhao, Z.,Wang, W.,Tang, Y.,Yang, X.,Guddat, L.W.,Liu, F.,Gao, Y.,Rao, Z.,Gong, H.
Structure of the human ATP synthase.
Mol.Cell, 83:2137-, 2023

PubMed Abstract: Biological energy currency ATP is produced by FF-ATP synthase. However, the molecular mechanism for human ATP synthase action remains unknown. Here, we present snapshot images for three main rotational states and one substate of human ATP synthase using cryoelectron microscopy. These structures reveal that the release of ADP occurs when the β subunit of FF-ATP synthase is in the open conformation, showing how ADP binding is coordinated during synthesis. The accommodation of the symmetry mismatch between F and F motors is resolved by the torsional flexing of the entire complex, especially the γ subunit, and the rotational substep of the c subunit. Water molecules are identified in the inlet and outlet half-channels, suggesting that the proton transfer in these two half-channels proceed via a Grotthus mechanism. Clinically relevant mutations are mapped to the structure, showing that they are mainly located at the subunit-subunit interfaces, thus causing instability of the complex.

PubMed: 37244256
DOI: 10.1016/j.molcel.2023.04.029

Experimental method

ELECTRON MICROSCOPY (2.61 Å)