Evidence and sources

Measurements

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Big picture numbers

Structures

• 8H9S
  Human F1Fo monomer, rotary state 1

  Most complete high-resolution mammalian F1Fo model: full c8 ring, subunit a, peripheral stalk and all nucleotides. Electron microscopy, 2.53 Å.
• 8H9T
  Human F1Fo, rotary state 2

  Second 120° rotary state of the same human enzyme; no IF1. Morph target from state 1. Electron microscopy, 2.77 Å.
• 8H9U
  Human F1Fo, rotary state 3a

  Third 120° rotary state; closes the three-state cycle for animation. Electron microscopy, 2.61 Å.
• 8H9V
  Human F1Fo, rotary substate 3b

  A substate inside one 120° step; shows that the rotor does not jump in one rigid move. Electron microscopy, 3.02 Å.
• 1BMF
  Bovine F1 head, crystal (classic)

  The structure that showed three β subunits in three different states, the basis of the rotary binding-change picture. X-ray diffraction, 2.85 Å.
• 2V7Q
  Bovine F1 inhibited by IF1

  Natural brake part: IF1 wedges into the βDP-αDP interface and blocks ATP hydrolysis. X-ray diffraction, 2.1 Å.
• 2XND
  Bovine F1-c8 rotor complex

  c-ring swap set, n = 8: the structure that established the c8 ring and H+/ATP = 2.7 in animal mitochondria. X-ray diffraction, 3.5 Å.
• 6CP6
  Yeast mitochondrial F1Fo monomer (c10)

  Fungal mitochondrial enzyme in a lipid bilayer, with a c10 ring instead of the animal c8. Electron microscopy, 3.6 Å.
• 6B8H
  Yeast mitochondrial F1Fo dimer

  Full dimer model: the V-shaped pair whose membrane subunits bend the inner membrane into cristae. The title says monomer, but the entry holds two copies of every subunit. Electron microscopy, 3.6 Å.
• 6OQR
  E. coli F1Fo (c10)

  The minimal bacterial enzyme (8 subunit types) with a c10 ring. Electron microscopy, 3.1 Å.
• 6N2Y
  Bacillus PS3 F1Fo (c10)

  Thermophilic bacterial enzyme; shows how ε blocks hydrolysis but allows synthesis. Electron microscopy, 3 Å.
• 6FKF
  Spinach chloroplast CF1Fo (c14)

  Plant enzyme with a large c14 ring (H+/ATP 4.7 by structure) and a redox off-switch. Electron microscopy, 3.15 Å.
• 7TMR
  Yeast V-ATPase (rotary pump)

  Evolution: the V-type relative that runs the rotary mechanism as an ATP-driven proton pump. Electron microscopy, 3.5 Å.
• 4V1G
  c9 ring, mycobacterial (H+)

  c-ring swap set, n = 9 (H+/ATP = 3.0). Drug-free partner of 4V1F. X-ray diffraction, 1.55 Å.
• 3U2F
  c10 ring, yeast mitochondria (H+)

  c-ring swap set, n = 10 (H+/ATP = 3.3). X-ray diffraction, 2 Å.
• 4BEM
  F/V hybrid ring, Acetobacterium woodii (Na+)

  c-ring swap set: 9:1 F/V hybrid with 10 Na+ sites; a link between synthases and pumps. X-ray diffraction, 2.1 Å.
• 1YCE
  c11 ring, Ilyobacter tartaricus (Na+)

  c-ring swap set, n = 11, the classic Na+ rotor. X-ray diffraction, 2.4 Å.
• 3ZK1
  c11 ring, Fusobacterium nucleatum (Na+)

  Second Na+ rotor with a two-carboxylate ion site, from a human pathogen. X-ray diffraction, 2.2 Å.
• 3ZO6
  c12 ring, engineered B. pseudofirmus (H+)

  c-ring swap set, n = 12: a point mutation shrinks the ring by one subunit. X-ray diffraction, 4.104 Å.
• 2X2V
  c13 ring, Bacillus pseudofirmus OF4 (H+)

  c-ring swap set, n = 13 (H+/ATP = 4.3), wild-type partner of the c12 mutant. X-ray diffraction, 2.5 Å.
• 6TQJ
  c14 ring, spinach chloroplast (H+)

  c-ring swap set, n = 14 (H+/ATP = 4.7). Higher resolution than 2W5J. X-ray diffraction, 2.3 Å.
• 2WIE
  c15 ring, Spirulina (Arthrospira) (H+)

  c-ring swap set, n = 15 (H+/ATP = 5.0), the largest ring in this set. X-ray diffraction, 2.13 Å.
• 2BL2
  K10 ring, V-type Na+-ATPase (Enterococcus hirae)

  Evolution comparison: a V-type rotor ring built from four-helix subunits. X-ray diffraction, 2.1 Å.
• 4V1F
  c9 ring + bedaquiline

  Drug swap: bedaquiline clamps every ion site of the mycobacterial c-ring. X-ray diffraction, 1.697 Å.
• 7JGC
  Mycobacterial Fo + bedaquiline

  Drug swap in context: bedaquiline pockets at the a/c interface of the intact Fo. Electron microscopy, 3.4 Å.
• 8KI3
  Human F1Fo + bedaquiline

  Same drug on the human enzyme: explains off-target binding; same chain lettering as the hero. Electron microscopy, 2.89 Å.
• 4F4S
  Yeast c10 ring + oligomycin A

  Drug swap: oligomycin binds the outer face of the c-ring at the proton site. X-ray diffraction, 1.9 Å.

References

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48. 48NIST CODATA value: Faraday constant