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Figure 4.
Figure 4. Structure of the Rab6-GCC185 Complex
(A)
Ribbon representation of the GCC185 Rab-binding domain dimer
(green) and Rab6 (blue) bound to GTP (stick model) and magnesium
(sphere). Switch I and II regions of Rab6 (Chattopadhyay et al.,
2000) are colored yellow and orange respectively.
(B) View
of the Rab6-GCC185-binding interface. A single GCC185 helix (E)
out of the two-fold symmetric coiled coil is shown for clarity.
Each helix contacts switch regions from two opposed Rab6
molecules A and B. Rab6 switch I and II (including W67) are
colored yellow and orange, respectively. Protein backbone
(α-carbon trace) and side chains involved in polar and
hydrophobic interactions are shown. Carbonyl oxygens are shown
for A44, I48, and I1588, and C-Cα bonds have been added to
simplify the figure. An anomalous difference Fourier density map
of the selenomethionine-substituted crystal (pink, contoured at
6σ) is shown for GCC185.
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