PDB file 1BMF
This structure of bovine mitochondrial F1 ATPase with bound nucleotides was solved by J. P. Abrahams, A. G. W. Leslie, R. Lutter, & J. E. Walker in 1996.
Suggested display options:
as ribbons and color chain to give each subunit a different color.
Rotate to view the complex looking at the ring of a & b subunits, along the axis of the g subunit helixes, and then with the g subunit "shaft" parallel to the screen.
Note how the bent helical loop of g extends up into the ring of a & b subunits.
Also view with the protein in spacefill display.
complex end on, with the g tail pointing out from the screen.
To make the protein disappear, select protein and then hide selected.
Select ligand, display as ball & stick, or spacefill, and color CPK.
For orientation and to visualize the g subunit, select *g and display as spacefill.
Identify the three catalytic b subunits by their variation in bound nucleotides.
With the nucleotides visible, bring back the rest of the protein by selecting protein, and display as wireframe.
Crystallographic data are consistent with a role of an
a-subunit arginine side-chain in adjusting the
position of the substrate/product water molecule at each b-subunit
active site depending on the presence or absence of the terminal phosphate of ATP.
Question: Is the location of each active site within the b-subunit consistent with such a role of the adjacent a subunit?
Return to Lecture
on F1Fo ATP Synthase
Or press Back button
at top twice
to return to your place in the notes.