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PDBsum entry 2xnd
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Contents |
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492 a.a.
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467 a.a.
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263 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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References listed in PDB file
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Key reference
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Title
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Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria.
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Authors
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I.N.Watt,
M.G.Montgomery,
M.J.Runswick,
A.G.Leslie,
J.E.Walker.
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Ref.
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Proc Natl Acad Sci U S A, 2010,
107,
16823-16827.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix
of the organelle, and is attached to the membrane domain by central and
peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is
provided by the transmembrane proton-motive-force across the inner membrane,
generated by respiration. The proton-motive force is coupled mechanically to ATP
synthesis by the rotation at about 100 times per second of the central stalk and
an attached ring of c-subunits in the membrane domain. Each c-subunit carries a
glutamate exposed around the midpoint of the membrane on the external surface of
the ring. The rotation is generated by protonation and deprotonation
successively of each glutamate. Each 360° rotation produces three ATP
molecules, and requires the translocation of one proton per glutamate by each
c-subunit in the ring. In fungi, eubacteria, and plant chloroplasts, ring sizes
of c(10)-c(15) subunits have been observed, implying that these enzymes need
3.3-5 protons to make each ATP, but until now no higher eukaryote has been
examined. As shown here in the structure of the bovine F(1)-c-ring complex, the
c-ring has eight c-subunits. As the sequences of c-subunits are identical
throughout almost all vertebrates and are highly conserved in invertebrates,
their F-ATPases probably contain c(8)-rings also. Therefore, in about 50,000
vertebrate species, and probably in many or all of the two million invertebrate
species, 2.7 protons are required by the F-ATPase to make each ATP molecule.
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