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Figure 5.
Figure 5. Structural Rearrangements Explain the Allosteric
Behavior of FabG
In the two panels, the α helices of
monomer A are orange, the β strands and coils of monomer A are
yellow, the α helices of monomer B are blue, and the β strands
and coils of monomer B are green.
(A) A close up of the
FabG intermonomer interface at region “c” as defined in
Figure 1B. Glu168′ from one monomer forms hydrogen bonds to
the amide nitrogens of Leu95 and Met96 on the adjacent monomer,
and residues N-terminal to Gly147 on the β5-α5 loop are
disordered.
(B) A close up of the same region in the
FabG·NADP^+ complex. Note that Glu168′ has shifted its
hydrogen bond register to the amide nitrogens of Leu95 and
Gly147, and the residues N-terminal to Gly147 on the β5-α5
loop are now ordered. The figure was produced using MOLSCRIPT
(Kraulis, 1991) and rendered with RASTER3D (Merritt and Murphy,
1994).
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