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Structural characteristics of yeast F1-ATPase before and after 16-degree rotation of the γ subunit: Theoretical analysis focused on the water-entropy effect
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10.1063/1.4734298
/content/aip/journal/jcp/137/3/10.1063/1.4734298
http://aip.metastore.ingenta.com/content/aip/journal/jcp/137/3/10.1063/1.4734298

Figures

Image of FIG. 1.
FIG. 1.

Summary of experimental results using the schematic representation of the αβγ complex viewed from the Fo side. (a) Schematic representation of the crystal structure. The scheme employed by Abrahams 11 is used for the naming of the α and β subunits. A yellow line represents that the packing in the two adjacent subunits is especially tight. 37 Three circular arcs denote sub-complexes I (black), II (blue), and III (red), respectively. The definition of each sub-complex is described in “Decomposition of αβγ complex into components.” The other figures represent (b) the overall configuration after the first 40° rotation of the γ subunit and (c) that after the second 80° rotation of the γ subunit. Primes are added to the subunits in (b) because their conformations should be different from those in (a). The arrow at the center of the γ subunit is defined in our previous paper. 23 Although ATP is bound to each of the three α subunits, it is not shown here.

Image of FIG. 2.
FIG. 2.

Changes in the system free energy during the 120° rotation of the γ subunit. “ATP hydrolysis” means the hydrolysis within β. “Configurational (structural) reorganization” means that of the αβγ complex.

Image of FIG. 3.
FIG. 3.

Schematic representation of the crystal structures of yeast F-ATPase. 13 Configurations (a) and (b) correspond to yF II and I, respectively. Relative to (a), the γ subunit of (b) rotates by 16° in the counterclockwise direction when it is viewed from the F side. Pi is bound to β in (a) while nothing is bound to that in (b), implying that Pi triggers the 16° rotation. Although ATP is bound to each of the three α subunits, it is not shown here.

Tables

Generic image for table
Table I.

Hydration free energy μ, entropy , and energy for a spherical solute with diameter 0.28 nm. 27 is the elementary electric charge.

Generic image for table
Table II.

Hydration entropy / and its change during the 16° rotation for each sub-complex defined in “Model and Theory.” “Before” and “After” correspond to yF II (before the rotation) and I (after the rotation), respectively. The column of “Change” shows the change in / caused by the rotation.

Generic image for table
Table III.

Change in the water-entropy gain upon the formation of each subunit pair during the 16° rotation (in ). The water-entropy gain is given as the difference between the hydration entropy of a subunit pair and the sum of the hydration entropies of separate subunits forming the pair (see Eq. (1) ).

Generic image for table
Table IV.

Change in the hydration entropy of each subunit during the 16° rotation (in ).

Generic image for table
Table V.

Hydration entropy / and its change during the 16° rotation for each sub-complex the γ subunit. “Before” and “After” correspond to yF II (before the rotation) and I (after the rotation), respectively. The column of “Change” shows the change in / caused by the rotation.

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/content/aip/journal/jcp/137/3/10.1063/1.4734298
2012-07-17
2014-04-20
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Structural characteristics of yeast F1-ATPase before and after 16-degree rotation of the γ subunit: Theoretical analysis focused on the water-entropy effect
http://aip.metastore.ingenta.com/content/aip/journal/jcp/137/3/10.1063/1.4734298
10.1063/1.4734298
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