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PDBsum entry 5fij
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Contents |
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509 a.a.
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480 a.a.
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467 a.a.
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264 a.a.
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131 a.a.
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47 a.a.
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(+ 2 more)
72 a.a.
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168 a.a.
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174 a.a.
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121 a.a.
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66 a.a.
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217 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-Em.
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Authors
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A.Zhou,
A.Rohou,
D.G.Schep,
J.V.Bason,
M.G.Montgomery,
J.E.Walker,
N.Grigorieff,
J.L.Rubinstein.
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Ref.
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Elife, 2015,
4,
e10180.
[DOI no: ]
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PubMed id
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Abstract
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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.
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