Figure 2.
Figure 2: Structural analysis of the GTPase reaction. a,
Comparison of the GppNHp circle
Mg^2+- binding pockets of hGBP1^LG (blue) and hGBP1^FL (yellow)
highlights the dimerization-induced reorientation of the
catalytic Arg 48 and Ser 73 side chains on their corresponding
loops. The grey van der Waals surface of monomer B (black)
from the hGBP1^LG circle
GppNHp dimer is shown to indicate how Arg 48 of monomer A would
clash with Thr 133 from monomer B. b, GDP circle
AlF[3] from the Ras circle
RasGAP complex^16 (orange) is superimposed on GDP circle
AlF[3] from hGBP1^LG (green), indicating that the cis 'arginine
finger' of hGBP1 (R48) has a similar orientation to that of the
trans arginine from RasGAP (R789).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2006,
440,
101-104)
copyright 2006.
circle
Mg^2+- binding pockets of hGBP1^LG (blue) and hGBP1^FL (yellow)
highlights the dimerization-induced reorientation of the
catalytic Arg 48 and Ser 73 side chains on their corresponding
loops. The grey van der Waals surface of monomer B (black)
from the hGBP1^LG