Figure 1.
Figure 1 The effect of domain swapping on the N-terminal hook
conformation in iNOS[ox]. Ribbon representation of the iNOS[ox]
dimer in swapped (A) and unswapped (B) conformations. N-terminal
hook regions (cyan and orange) interact primarily with their own
subunits (purple and red) in the unswapped conformation, but
reach across to associate with the opposite subunit in the
swapped conformation. Each heme (yellow bonds) is cupped in the
inward-facing palm of the central webbed -sheet
of the 'catcher's mitt' subunit fold. A self-symmetric disulfide
bond (yellow, bottom center) links the two subunits in the
swapped conformation (A). A single zinc ion (gray, bottom
center) is bound between the two subunits at the base of the
catcher's mitts in the unswapped conformation (B). Two molecules
of H[4]B (yellow, center, on edge) are also bound at the
interface and line the active-center channels leading to the
hemes.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
6271-6281)
copyright 1999.
-sheet
of the 'catcher's mitt' subunit fold. A self-symmetric disulfide
bond (yellow, bottom center) links the two subunits in the
swapped conformation (A). A single zinc ion (gray, bottom
center) is bound between the two subunits at the base of the
catcher's mitts in the unswapped conformation (B). Two molecules
of H[4]B (yellow, center, on edge) are also bound at the
interface and line the active-center channels leading to the
hemes.