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8FL8

Yeast ATP Synthase structure in presence of MgATP

Summary for 8FL8
Entry DOI10.2210/pdb8fl8/pdb
EMDB information29270 29278
DescriptorATP synthase protein 8, ATP synthase subunit a, ATP synthase subunit 4, mitochondrial, ... (17 entities in total)
Functional Keywordsf-type, atp synthase, yeast, mitochondrial, membrane protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains27
Total formula weight554731.31
Authors
Sharma, S.,Patel, H.,Luo, M.,Mueller, D.M.,Liao, M. (deposition date: 2022-12-21, release date: 2024-01-17, Last modification date: 2024-05-01)
Primary citationSharma, S.,Luo, M.,Patel, H.,Mueller, D.M.,Liao, M.
Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F 1 -F o coupling.
Nat.Struct.Mol.Biol., 31:657-666, 2024
Cited by
PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase uses the proton gradient across the inner mitochondrial membrane to synthesize ATP. Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the mitochondrial matrix is slightly acidic during hypoxia and pH-dependent conformational changes in the ATP synthase have been reported. Here we use single-particle cryo-EM to analyze the conformational ensemble of the yeast (Saccharomyces cerevisiae) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
PubMed: 38316880
DOI: 10.1038/s41594-024-01219-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.2 Å)
Structure validation

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