|
Figure 5.
Fig. 5. Comparison of the putative effector-binding
cavity of the tyrosine- and phenylalanine-regulated DAHP
synthases. (A) Amino acid sequence alignment of a part of the
putative regulation cavity of the tyrosine- and
phenylalanine-regulated DAHP synthases of several organisms. C.
albicans, Candida albicans; A. nidulans, Aspergillus nidulans;
H. influenzae, Haemophilus influenzae; S. typhimurium,
Salmonella typhimurium. (B-D) Accessible surface plots of the
tyrosine-regulated DAHP synthase Aro4p from S. cerevisiae (S.c.,
B and C) and the phenylalanine-inhibited DAHP synthase AroG from
E. coli (E.c., D). Surface elements closer than 3 Å to
atoms belonging to the N-terminal extension or the inserted  sheet are
shown in cyan. Residues identified as playing a role in
regulation (blue) and for the specificity-related residue (red,
G226 in Aro4p and S211 in AroG) are indicated. (B) The
orientation is the same as described for Fig. 2B. (C and D) The
view is rotated by 40° around the vertical and 30°
around the horizontal axis with respect to Fig. 2B. The figure
was created with DINO (ref. 23 and www.dino3d.org).
|
