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Figure 7.
Figure 7. The uncomplexed tryptase single mutant rHTaG. (a)
Stick representation of the active site of rHTaG, showing the
open conformation (  vert,
similar 75% occupancy, blue) and the closed conformation ( vert,
similar 25% occupancy, light blue) as thick sticks.
Additionally, the 214-220 segments of aI-tryptase (orange) and
bII-tryptase (green) are superimposed as thin stick models to
show the high level of similarity of both conformations with the
two conformations seen in free active rHTaG. (b) B-factors of
the inhibited single mutant rHTaGI (continuous line), of the
inhibited double mutant rHTaQGI (dotted line) and of the
uncomplexed single mutant rHTaG (broken line) are plotted
against residue number (chymotrypsinogen numbering). A striking
increase of the B-factors can be seen for the 214-220 segment of
rHTaG. (c) Electron density of an averaged kicked omit map
(orange mesh) shown together with the open (blue) and the closed
(light blue) conformation of the 214-220 segment. The map was
calculated for residues 214-220 in the closed conformation and
contoured at 1.8s. The active site residues are shown in green.
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