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PDBsum entry 5lqx
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Contents |
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30 a.a.
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25 a.a.
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17 a.a.
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27 a.a.
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503 a.a.
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471 a.a.
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267 a.a.
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128 a.a.
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57 a.a.
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43 a.a.
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(+ 4 more)
73 a.a.
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163 a.a.
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154 a.a.
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145 a.a.
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21 a.a.
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122 a.a.
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44 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 of the mitochondrial ATP synthase from pichia angusta determined by electron cryo-Microscopy.
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Authors
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K.R.Vinothkumar,
M.G.Montgomery,
S.Liu,
J.E.Walker.
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Ref.
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Proc Natl Acad Sci U S A, 2016,
113,
12709-12714.
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PubMed id
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Abstract
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The structure of the intact monomeric ATP synthase from the fungus, Pichia
angusta, has been solved by electron cryo-microscopy. The structure provides
insights into the mechanical coupling of the transmembrane proton motive force
across mitochondrial membranes in the synthesis of ATP. This mechanism requires
a strong and integral stator, consisting of the catalytic
α3β3-domain, peripheral stalk, and, in the membrane
domain, subunit a and associated supernumerary subunits, kept in contact with
the rotor turning at speeds up to 350 Hz. The stator's integrity is ensured by
robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to
the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8
subunit provides an additional brace between the peripheral stalk and subunit a.
At the junction between the OSCP and the apparently stiff, elongated α-helical
b-subunit and associated d- and h-subunits, an elbow or joint allows the stator
to bend to accommodate lateral movements during the activity of the catalytic
domain. The stator may also apply lateral force to help keep the static
a-subunit and rotating c10-ring together. The interface between the
c10-ring and the a-subunit contains the transmembrane pathway for
protons, and their passage across the membrane generates the turning of the
rotor. The pathway has two half-channels containing conserved polar residues
provided by a bundle of four α-helices inclined at ∼30° to the plane of the
membrane, similar to those described in other species. The structure provides
more insights into the workings of this amazing machine.
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