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Figure 4.
Figure 4. The Crystal Structure of the R2i-R LBD Reveals
Closely Opposed Arg743 Side Chains; C ζ Distance = 3.9 Å
(A) Sequence alignment depicting amino acid changes between
flip and flop, starting at position 744; the R/G site (743) is
shown in bold. Alternative residues are indicated in color.
Helices J and K (light blue bars) are drawn above the sequences.
Note that the cluster of changes comprising position 775–779
is not included in the structure.
(B) Side view of the
glutamate-bound flip/R LBD dimer. The two subunits are color
coded (chain A in cyan, chain C in yellow). Arg743 is indicated
in stick.
(C) Superposition of the flip/R (yellow) and
flop/G LBDs (gray; top view). Alternative residues, 743–745,
are shown in stick: flip residues, black; flop residues, white;
positions are indicated on one protomer only. Helices D and J
are denoted.
(D) Fo-Fc electron densities for Arg743 side
chains. Contour level was 0.16 e/Å^3. The figure was drawn
with CCP4mg.
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