1. Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites 
R.Ian Menz, John E. Walker, Andrew G.W. Leslie 
Cell 
Volume 106, Issue 3, Pages (August 2001)
DOI: /S (01)

2. Figure 1
Conformational Changes due to Nucleotide Binding in the βE Subunit of Bovine F1-ATPase
(a) Difference electron density for ADP, sulfate, and magnesium bound to the βE subunit of (ADP.AlF4−)2F1. The electron density was calculated with model phases before inclusion of ADP, Mg, or SO4 in the model. Contours are drawn at 3σ. Parts (b) and (c) show space filling representations of the αE (red) and βE (yellow) subunits in the native structure (b) and the (ADP.AlF4−)2F1 structure (c). In (c), the nucleotide is shown in magenta. (d) Ribbon representation of the βADP+Pi subunit (red) superimposed on the βE subunit (green) of the native structure and (e) on the βDP subunit (green) of the (ADP.AlF4−)2F1 structure. The γ subunit of the (ADP.AlF4−)2F1 structure is shown in blue. For clarity, the γ subunit of the native structure is not shown. The rotation axis that relates the two conformations of the lower region of the nucleotide binding domains and C-terminal domains is drawn in black
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3. Figure 2
The Coordination of Aluminium Fluoride in the Catalytic Sites of Bovine F1-ATPase
(a) Residues involved in nucleotide binding and catalysis and the elements of secondary structure in the βDP subunit of the (ADP.AlF4−)2F1 structure. Atom colors are yellow (carbon), blue (nitrogen), red (oxygen), pink (fluoride), magenta (phosphorous), orange (magnesium), and gray (aluminium). (b–d) Schematic representations of the coordination of the aluminium fluoride group bound to the catalytic sites of (b) the βDP subunit of the (ADP.AlF4−)2F1 structure, (c) the βDP subunit of the (ADP.AlF3)F1 structure, and (d) the βTP subunit of the (ADP.AlF4−)2F1 structure. Possible hydrogen bond interactions are shown as dotted lines. All distances are in Å
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4. Figure 3 Comparison of the Catalytic Sites in Bovine F1-ATPase
(a) Space filling representations of the catalytic interface of the βTP and βDP subunits in the (ADP.AlF4−)2F1 structure. The α subunits are shown in red, the β subunits in yellow, and the bound nucleotide in magenta. (b–d) Stereo views of the residues involved in nucleotide binding and catalysis and the elements of secondary structure in this region following superposition of residues β152–172.
(b) Comparison of the βTP site (drawn with colored atoms and bonds and blue main chain ribbon) and the βDP site (gray atoms, bonds, and main chain).
(c and d) The βADP+Pi subunit (drawn with colored atoms and bonds and blue main chain ribbon) is shown superposed on (c) the closed conformation of the βDP subunit (gray atoms, bonds, and main chain) and (d) the open conformation of the βE subunit (gray atoms, bonds, and main chain). The P loop lies between the C-terminal end of β strand 3 and the α helix B. Hydrogen bonds to the sulfate group are drawn as dotted lines in (d). Atom colors as in Figure 2a, and green (sulfur)
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5. Figure 4
A Scheme for the Binding Change Mechanism of Catalysis in F1-ATPase at Saturating Concentrations of ATP Based on the Bovine Crystal Structures
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6. Figure 5 Rotation of the γ Subunit in Bovine F1-ATPase
Stereo view of part of the γ subunit (residues 3–35 and 221–250) and the C-terminal domains of the (αβ)3 hexamer in the native structure (blue) and the (ADP.AlF4−)2F1 structure (red), following superposition of the N-terminal domains. The βE subunit shows the largest conformational change, but the rotation of the γ subunit is also apparent. Note that interacting residues in the βE subunit and the γ subunit move in opposite directions
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7. Figure 6
A Model for the Generation of Rotation of the γ Subunit during ATP Hydrolysis in F1-ATPase
The structures of the C-terminal domains of the α and β subunits are shown in red (pink shading) and yellow (yellow shading), respectively. The coiled-coil region of the γ subunit (residues 3–35 and 221–250) that is in contact with the C-terminal domains is shown in blue (blue shading). The nucleotide binding sites are shown in green. The structure of the native enzyme is shown in (a) and (c), and the (ADP.AlF4−)2F1 structure is shown in (b)
Cell  , DOI: ( /S (01) )