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Figure 1.
Figure 1. The overall fold of the ncd dimer. (a) Schematic
representation of the ncd conformation and of the polypeptide
chain with the secondary structure elements visible in the
crystal structure, following the nomenclature in [9]. The
sequence in the coiled-coil helix is shown below. (b) Stereoview
of the C[a] backbone of the Drosophila melanogaster ncd dimer 1.
Every twentieth residue and also the N termini (N) and the C
termini of the two head domains are labelled. (c) Stereoview of
the structure of dimer 1. Helices of the first head domain are
coloured in orange and b strands are in light blue. In the
second head domain, helices are in red and b strands are dark
blue. The MgADP in the active site is shown as a ball-and-stick
model. This and the following figures were prepared with the
program MOLSCRIPT [32].
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