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Figure 2.
Figure 2. Molecular architecture of G203AG[iα1]. (a) Helical
segments are shown as green ribbons and β strands as blue
arrows; secondary structural elements near the catalytic site
are labeled, GDP and Pi are shown as ball-and-stick models.
Switch regions (Sw) are labeled (I–IV) and ‘N’ and
‘C’ mark the locations of residues 34 and 343, respectively.
(b) A superposition of the Cα traces of the G[iα1] subunit
bound to GDP (blue), G[iα1]bound to GTPγS–Mg^2+ (red), and
the GDP–Pi complex of G203AG[iα1] (green). The Cα atoms of
residues 40–178 and 220–340 were used to generate the
superposition. Figure 2. Molecular architecture of
G203AG[iα1]. (a) Helical segments are shown as green ribbons
and β strands as blue arrows; secondary structural elements
near the catalytic site are labeled, GDP and Pi are shown as
ball-and-stick models. Switch regions (Sw) are labeled
(I–IV) and ‘N’ and ‘C’ mark the locations of residues
34 and 343, respectively. (b) A superposition of the Cα traces
of the G[iα1] subunit bound to GDP (blue), G[iα1]bound to
GTPγS–Mg^2+ (red), and the GDP–Pi complex of G203AG[iα1]
(green). The Cα atoms of residues 40–178 and 220–340 were
used to generate the superposition. (Figure was generated using
the program SETOR [[3]55].)
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