Figure 3.
FIG. 3. The [2Fe-2S] cluster at the center of the GABA-AT
dimer. A, structure of the GABA-AT dimer. The view is
approximately along the molecular 2-fold symmetry axis. The C
traces of the two
subunits are shown in black and red. Helix 5 and its symmetry
mate are highlighted by thick gray traces. The [2Fe-2S] cluster
on the molecular 2-fold symmetry axis together with the
liganding cysteines and the two symmetry related PLP cofactors
are shown in full view. B, close-up view of A. The C traces
have been omitted for clarity. Symmetry-related residues are
marked with the symbol "#." C, stereographic close-up view. The
molecular 2-fold axis is approximately along the vertical
direction. The native 2F[o] - F[c] omit map (magenta; contour
level 1.2 ) and the anomalous
difference map (light blue; contour level 4.5 ) were
computed with data to 2.3-Å resolution (data set of the
vigabatrin complex). The iron and sulfur atoms were not included
for phasing.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
363-373)
copyright 2004.
traces of the two
subunits are shown in black and red. Helix 5 and its symmetry
mate are highlighted by thick gray traces. The [2Fe-2S] cluster
on the molecular 2-fold symmetry axis together with the
liganding cysteines and the two symmetry related PLP cofactors
are shown in full view. B, close-up view of A. The C 
) and the anomalous
difference map (light blue; contour level 4.5