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Title
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Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.
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Authors
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V.Kabaleeswaran,
N.Puri,
J.E.Walker,
A.G.Leslie,
D.M.Mueller.
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Ref.
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EMBO J, 2006,
25,
5433-5442.
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PubMed id
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Abstract
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The crystal structure of yeast mitochondrial F(1) ATPase contains three
independent copies of the complex, two of which have similar conformations while
the third differs in the position of the central stalk relative to the
alpha(3)beta(3) sub-assembly. All three copies display very similar asymmetric
features to those observed for the bovine enzyme, but the yeast F(1) ATPase
structures provide novel information. In particular, the active site that binds
ADP in bovine F(1) ATPase has an ATP analog bound and therefore this structure
does not represent the ADP-inhibited form. In addition, one of the complexes
binds phosphate in the nucleotide-free catalytic site, and comparison with other
structures provides a picture of the movement of the phosphate group during
initial binding and subsequent catalysis. The shifts in position of the central
stalk between two of the three copies of yeast F(1) ATPase and when these
structures are compared to those of the bovine enzyme give new insight into the
conformational changes that take place during rotational catalysis.
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