|
Figure 3.
Figure 3. Ribbon diagrams of CheY in stereo showing
movement of side-chains Thr87 and Tyr106 upon activation.
Superposition included backbone coordinates for residues in H1,
H2, b1, b2, and b3. Relative that depicted in Figure 2, the
structures are rotated 90° about a horizontal axis in the
page, affording a view (top) of the active site. The loops
between b3 and H3 and between H3 and b4 are ill-defined by the
NMR data, and should not be used for comparison. (a) CheY taken
from the inactive magnesium-bound NMR structure [Moy et al 1994]
and (b) representative NMR structure of BeF[3]-activated CheY.
Asp57 (blue) is the site of phosphorylation. Highly conserved
Tyr106 (green) and Thr87 (red) are also shown. The Thr87
hydroxyl group is represented by a small ball. BeF[3]^ - is
modeled as a black ball attached to Asp57. The Figure was
created with the program MOLSCRIPT [Kraulis 1991].
|
