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Basic information
Entry | Database: EMDB / ID: EMD-3169 | |||||||||
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Title | Bovine mitochondrial ATP synthase state 3a | |||||||||
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![]() | Bovine mitochondrial ATP synthase: ATP synthase ![]() | |||||||||
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Function / homology | ![]() proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial envelope / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / ATP biosynthetic process / proton transmembrane transport / mitochondrial ATP synthesis coupled proton transport ...proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase, stator stalk / mitochondrial proton-transporting ATP synthase complex assembly / mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial envelope / mitochondrial proton-transporting ATP synthase complex / mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) / ATP biosynthetic process / proton transmembrane transport / mitochondrial ATP synthesis coupled proton transport / proton-transporting ATP synthase complex, coupling factor F(o) / proton-transporting ATP synthase complex, catalytic core F(1) / ATP synthesis coupled proton transport / proton transmembrane transporter activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Zhou A / Rohou A / Schep DG / Bason JV / Montgomery MG / Walker JE / Grigorieff N / Rubinstein JL | |||||||||
![]() | ![]() Title: Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. Authors: Anna Zhou / Alexis Rohou / Daniel G Schep / John V Bason / Martin G Montgomery / John E Walker / Nikolaus Grigorieff / John L Rubinstein / ![]() ![]() ![]() Abstract: Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic ...Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases. | |||||||||
Validation Report | PDB-ID: 5fik![]() ![]() ![]() | |||||||||
History |
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Structure visualization
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Header (meta data in XML format) |
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Images |
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Archive directory |
-Related structure data
Related structure data | ![]() 5fikCM ![]() 3164C ![]() 3165C ![]() 3166C ![]() 3167C ![]() 3168C ![]() 3170C ![]() 3181C ![]() 5araC ![]() 5areC ![]() 5arhC ![]() 5ariC ![]() 5fijC ![]() 5filC C: citing same article ( M: atomic model generated by this map |
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Similar-shape strucutres |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.64 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire Bovine mitochondrial ATP synthase
Entire | Name: Bovine mitochondrial ATP synthase / Details: Detergent-solubilized protein complex / Number of components: 1 Oligomeric State: One hetero-oligomeric ATP synthase complex |
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Mass | Experimental: 600 kDa |
-Component #1: protein, ATP synthase
Protein | Name: ATP synthase![]() ![]() |
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Mass | Experimental: 600 kDa |
Source | Species: ![]() ![]() ![]() |
Source (natural) | Organelle: Mitochondria / Location in cell: Mitochondrial membrane / Organ or tissue: Heart |