ATP synthase is a membrane protein complex that synthesizes ATP. ATP synthase is composed of several subunits that work together to produce ATP. In this model, ADP molecules are bound to all catalytic and non-catalytic subunits. A phosphate is bound to one of the catalytic sites adopting a half-closed conformation just before release of ATP.
This model was created using ChimeraX from cryo-EM and x-ray crystallography structure data in the Protein Data Bank (PDB ID 5ARI & 1H8E). PDB DOI: 10.2210/pdb5ARI/pdb & 10.2210/pdb1H8E/pdb & https://www.cgl.ucsf.edu/chimerax/
Zhou A et al. (2015). Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. Elife 6;4:e10180. doi: 10.7554/eLife.10180. PMID: 26439008; PMCID: PMC4718723.
Menz RI et al. (2001). Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis. Cell 10; 106(3): 331-41. doi: 10.1016/s0092-8674(01)00452-4. PMID: 11509182.
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