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TitleStructure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.
Journal, issue, pagesElife, Vol. 4, Page e10180, Year 2015
Publish dateOct 6, 2015
AuthorsAnna Zhou / Alexis Rohou / Daniel G Schep / John V Bason / Martin G Montgomery / John E Walker / Nikolaus Grigorieff / John L Rubinstein /
PubMed AbstractAdenosine 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.
External linksElife / PubMed:26439008 / PubMed Central
MethodsEM (single particle)
Resolution6.4 - 9 Å
Structure data

EMDB-3164, PDB-5ara:
Bovine mitochondrial ATP synthase state 1a
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-3165, PDB-5are:
Bovine mitochondrial ATP synthase state 1b
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-3166, PDB-5arh:
Bovine mitochondrial ATP synthase state 2a
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-3167, PDB-5ari:
Bovine mitochondrial ATP synthase state 2b
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-3168, PDB-5fij:
Bovine mitochondrial ATP synthase state 2c
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-3169, PDB-5fik:
Bovine mitochondrial ATP synthase state 3a
Method: EM (single particle) / Resolution: 6.4 Å

EMDB-3170, PDB-5fil:
Bovine mitochondrial ATP synthase state 3b
Method: EM (single particle) / Resolution: 7.1 Å

EMDB-3181:
Average of seven maps of the bovine mitochondrial ATP synthase with Fo regions aligned
Method: EM (single particle) / Resolution: 9 Å

Source
  • bos taurus (cattle)
KeywordsATP synthase / rotary ATPase / Animals / Cattle / Computational Biology / Cryoelectron Microscopy / Imaging, Three-Dimensional / Mitochondrial Proton-Translocating ATPases / Models, Molecular / Protein Conformation / Protein Folding / HYDROLASE

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