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Figure 4.
Figure 4. The external nucleotide-binding site. (a) Omit
F[o]–F[c] electron density at the external nucleotide-binding
site, contoured at 3 σ (blue) and 7.5 σ (black). The density,
located between motifs II and III of FtsY (below, purple) and
the closing loop of Ffh (above), enters the water-filled channel
that abuts the shared active site chamber,^13 and is close to
both active site nucleotides (shown ”ghosted”). (b) Stereo
view of the hydrogen bonding interactions between the external
GMP molecule and residues and water molecules at the complex
interface are shown in an orientation similar to that in (a).
Key water molecules are shown as larger spheres and labeled as
in Figure 2(c). Ffh residues are highlighted in grey, FtsY
residues in purple, and motifs I, II and III are labeled. Phe141
participates in π-π stacking interactions with the purine
ring of the GMP molecule (front, center). Figure 4. The
external nucleotide-binding site. (a) Omit F[o]–F[c] electron
density at the external nucleotide-binding site, contoured at 3
σ (blue) and 7.5 σ (black). The density, located between
motifs II and III of FtsY (below, purple) and the closing loop
of Ffh (above), enters the water-filled channel that abuts the
shared active site chamber,[3]^13 and is close to both active
site nucleotides (shown ”ghosted”). (b) Stereo view of the
hydrogen bonding interactions between the external GMP molecule
and residues and water molecules at the complex interface are
shown in an orientation similar to that in (a). Key water
molecules are shown as larger spheres and labeled as in
[4]Figure 2(c). Ffh residues are highlighted in grey, FtsY
residues in purple, and motifs I, II and III are labeled. Phe141
participates in π-π stacking interactions with the purine ring
of the GMP molecule (front, center).
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