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1QO1

Molecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria

Summary for 1QO1
Entry DOI10.2210/pdb1qo1/pdb
Related1A91 1AQT 1BMF 1BSH 1BSN 1COW 1EFR 1NBM
DescriptorATP SYNTHASE ALPHA CHAIN, ATP SYNTHASE BETA CHAIN, ATP SYNTHASE GAMMA CHAIN, ... (5 entities in total)
Functional Keywordsatp synthase, low resolution model, c-alpha only
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Total number of polymer chains18
Total formula weight448851.35
Authors
Stock, D.,Leslie, A.G.W.,Walker, J.E. (deposition date: 1999-11-01, release date: 1999-11-04, Last modification date: 2023-12-13)
Primary citationStock, D.,Leslie, A.G.W.,Walker, J.E.
Molecular Architecture of the Rotary Motor in ATP Synthase
Science, 286:1700-, 1999
Cited by
PubMed Abstract: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
PubMed: 10576729
DOI: 10.1126/SCIENCE.286.5445.1700
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.9 Å)
Structure validation

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