Figure 1.
Figure 1. Structures of the GGA1-GAT domain and its complex with
ARF1. a, Stereo diagram of the GGA1-GAT domain. The GAT
domain forms three -helices
connected by loops of varying length. The final model is
complete except for the N-terminal 26 residues (166 -191, dotted
line) and the C-terminal 2 residues (304 -305), whose electron
density is weak. b, Stereo view of the omit F[o] -F[c] electron
density map of the GGA1 N-GAT (Leu178 -Asn194) within the ARF1
-N-GAT complex. The map was calculated to 1.6 Å resolution and
is displayed at 1.5 cutoff,
superimposed with a ball-and-stick model of the N-GAT domain. c,
Stereo view of the ARF1 -N-GAT complex. N-GAT forms a
helix-loop-helix motif facing switches 1 and 2 of ARF1-GTP. The
diagrams in (a) and (c) are shown in the same orientation, which
was chosen by the least-square minimization of the overlap of a
common helical region (199 -205, shown in red in a and c)
between the GAT domain and the ARF1 -N-GAT complex.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2003,
10,
386-393)
copyright 2003.
-helices
connected by loops of varying length. The final model is
complete except for the N-terminal 26 residues (166 -191, dotted
line) and the C-terminal 2 residues (304 -305), whose electron
density is weak. b, Stereo view of the omit F[o] -F[c] electron
density map of the GGA1 N-GAT (Leu178 -Asn194) within the ARF1
-N-GAT complex. The map was calculated to 1.6 Å resolution and
is displayed at 1.5 
cutoff,
superimposed with a ball-and-stick model of the N-GAT domain. c,
Stereo view of the ARF1 -N-GAT complex. N-GAT forms a
helix-loop-helix motif facing switches 1 and 2 of ARF1-GTP. The
diagrams in (a) and (c) are shown in the same orientation, which
was chosen by the least-square minimization of the overlap of a
common helical region (199 -205, shown in red in a and c)
between the GAT domain and the ARF1 -N-GAT complex.