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PDBsum entry 3k5b
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References listed in PDB file
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Key reference
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Title
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The structure of the peripheral stalk of thermus thermophilus h+-Atpase/synthase.
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Authors
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L.K.Lee,
A.G.Stewart,
M.Donohoe,
R.A.Bernal,
D.Stock.
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Ref.
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Nat Struct Biol, 2010,
17,
373-378.
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PubMed id
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Abstract
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Proton-translocating ATPases are ubiquitous protein complexes that couple ATP
catalysis with proton translocation via a rotary catalytic mechanism. The
peripheral stalks are essential components that counteract torque generated from
proton translocation during ATP synthesis or from ATP hydrolysis during proton
pumping. Despite their essential role, the peripheral stalks are the least
conserved component of the complexes, differing substantially between subtypes
in composition and stoichiometry. We have determined the crystal structure of
the peripheral stalk of the A-type ATPase/synthase from Thermus thermophilus
consisting of subunits E and G. The structure contains a heterodimeric
right-handed coiled coil, a protein fold never observed before. We have fitted
this structure into the 23 A resolution EM density of the intact A-ATPase
complex, revealing the precise location of the peripheral stalk and new
implications for the function and assembly of proton-translocating ATPases.
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