Figure 6.
Figure 6. The hexameric T3SS and F1 ATPases. Right, the [3]
[3]
heterohexamer of the F1 ATPase, with known membrane orientation
delineated by the binding of its membrane-anchored -subunit
(purple) within the inner pore of the ATPase hexameric ring. In
yellow is the helical domain at the C terminus of the F1
ATPases, which is absent in EscN. Left, the EscN homohexamer
(blue), with the predicted docking site for the helical T3SS
chaperone (PDB 1XKP^41; red), in complex with its cognate and
partially unfolded effector (green). The functional point
mutation V393P lies at the edge of the chaperone-binding surface
(yellow).
[3]
[3]
heterohexamer of the F1 ATPase, with known membrane orientation
delineated by the binding of its membrane-anchored 
-subunit
(purple) within the inner pore of the ATPase hexameric ring. In
yellow is the helical domain at the C terminus of the F1
ATPases, which is absent in EscN. Left, the EscN homohexamer
(blue), with the predicted docking site for the helical T3SS
chaperone (PDB 1XKP^41; red), in complex with its cognate and
partially unfolded effector (green). The functional point
mutation V393P lies at the edge of the chaperone-binding surface
(yellow).