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Figure 2.
Fig. 2. Aro4p structure of S. cerevisiae. (A) Topology
plot of DAHP synthase from S. cerevisiae. The  -strands and
 -helices of
the central / barrel are
shown in orange and yellow, respectively. Loops on the N- and
C-terminal sides of the barrel are in cyan and green,
respectively. The additional structural elements at the N
terminus and between helix 5 and -strand 6 are also
shown in cyan. Residues involved in binding of PEP are marked in
green. Residues involved in regulation are marked in blue with
italic lettering for those identified by random screening and
normal lettering for those found by site-directed mutagenesis.
Red arrows mark the cutting points in Aro4p for the chimera
constructs (Fig. 1A). The dotted 0 strand is
part of the second monomer of a dimer and interacts with the
6a and 6b. (B) The
crystal structure of DAHP synthase from S. cerevisiae in ribbon
presentation. The crystal structures contain a molecule of PEP
bound to the active site shown as space-filling models (red and
magenta). Secondary structure elements are color-coded as
described for A. Shown are views from the C-terminal face of the
central barrel
(Left), side of the barrel (Center), and N-terminal face of the
barrel (Right). The programs MOLSCRIPT 2.1 (21) and RASTER3D
(22) were used for the presentation of DAHP synthase.
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