|
Figure 1.
Figure 1. Structure of the ARL2-GTP-BART Complex
(A) A
stereo view of the ARL2-GTP-BART complex. ARL2 is colored in
yellow with the N-terminal α helix in cyan and the switch I,
switch II, and inter-switch regions in magenta, orange, and
blue, respectively. The bound GTP is shown with a ball-and-stick
model and the Mg^2+ ion in a green sphere. BART is colored in
green with the secondary structures labeled.
(B) A stereo
view of a representative difference Fourier Fo-Fc map (2σ
contour level) in the interaction interface of the ARL2-BART
complex in the region of helix α1 of ARL2 and helix α4 of
BART.
(C) Superposition of ARL2-GTP in the ARL2-GTP-BART
(red) and ARL2-GTP-PDEδ complexes (blue) and ARL3-GDP (yellow)
showing the overall conformational differences.
(D)
Superposition of the crystal structure of BART in the
ARL2-GTP-BART complex (green) and the NMR solution structure of
BART alone (yellow) showing the overall conformational
differences.
|
