Fig. 1. Structural overview. (A) Cartoon representation of
mFAS, colored by domains as indicated. Linkers and linker
domains are depicted in gray. Bound NADP^+ cofactors and the
attachment sites for the disordered C-terminal ACP/TE domains
are shown as blue and black spheres, respectively. The position
of the pseudo-twofold dimer axis is depicted by an arrow;
domains of the second chain are indicated by an appended prime.
The lower panel (front view) shows a corresponding schematic
diagram. (B) Top (upper panel) and bottom (lower panel) views,
demonstrating the "S" shape of the modifying (upper) and
condensing (lower) parts of mFAS. The pseudo-twofold axis is
indicated by an ellipsoid. (C) Linear sequence organization of
mFAS, at approximate sequence scale.
The above figure is reprinted
by permission from the AAAs: