Structure of F1-ATP ase from beef heart mitochondria


In the initial view, the crystallographic structure is shown as a Ca-backbone, with the subunits colored by chain. The bound nucleotides are shown as wireframe models, colored blue. The g-subunit projects from the cylinder formed by the 3 a, b-subunits at the bottom, which is the interface with Fo.

The protein, showing subunits

Click here to reset to original view, with backbone structure.
  1. The protein structure is shown as a Ca-backbone, colored by chain. Chains A, B, and C are a-subunits, colored dark-blue, blue, blue-green; chains D, E, F are b-subunits, colored green, green-yellow, yellow. The g-subunit is red. Nucleotides are shown as spacefilling models. Chain D (green) is bDP, and has a bound ADP; Chain E (green-yellow), which has no bound nucleotide, is subunit bE; Chain F (yellow) is bTP, and has a bound AMP-PNP. The a-subunits all have bound AMP-PNP (as an ATP analogue).
  2. Richardson cartoon of the protein, showing secondary structure, colored by chain. Chains A, B, and C are a-subunits, colored dark-blue, blue, blue-green; chains D, E, F are b-subunits, colored green, green-yellow, yellow. Bound nucleotides are shown as wireframe models.
  3. Please turn rotation off before going any further.

  4. The protein structure is shown as a spacefilling model, colored by chain. To view structure from the top, click on Rotate 90o about x-axis button below. Chains A, B, and C are a-subunits, colored dark-blue, blue, blue-green; chains D, E, F are b-subunits, colored green, green-yellow, yellow. The g-subunit is red.
  5. Set slabmode on (click on image with right mouse button to get menu; options) to see a slice through the structure. The depth is at about the level of the nucleotide binding domains. See frame at left for instructions.

  6. Rotate 90o about x-axis. Rotate -90o about x-axis.
  7. Rotate 90o about y-axis. Rotate -90o about y-axis.
  8. Rotate 90o about z-axis. Rotate -90o about z-axis.

The g-subunit, and its role as an axle for the a,b-subunits.

Click here to reset to original view, with backbone structure.
  1. View the g-subunit as a spacefilling model.
  2. Color g-subunit by residue polarity. Hydrophobic residues are white, neutral polar residues are green, basic residues are blue, acidic residues are red.
  3. Color the a,b-subunits by residue polarity. Hydrophobic residues are white, neutral polar residues are green, basic residues are blue, acidic residues are red.

The conformation of the b-subunits.

  1. The b-subunits in cartoon, showing the different conformations with occupancy of the nucleotide binding site. Colors are as for 1 above. ANP-PNP shown white, ADP shown blue
  2. See bDP alone.
  3. See bE alone.
  4. See bTP alone.
  5. See ATP-binding site in bTP. The backbone is colored blue, atoms within 6.0 Å of the AMP-PNP are colored by CPK atom colors; the AMP-PNP is colored yellow. Waters are green. Click here to see the AMP-PNP colored by CPK atom colors.

References

  1. Abrahams, J.P., Leslie, A.G., Lutter, R. and Walker, J.E. (1994) Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370, 621-628

©Copyright 1996, Antony Crofts, University of Illinois at Urbana-Champaign, a-crofts@uiuc.edu