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Figure 1.
Figure 1. Structure of p97 D2 at 3.0 Å Resolution
(A) The heptameric state of p97 D2 is shown as crystallized.
Protomers are uniquely colored.
(B) Schematic of
transformations mapping D2 protomer from hepatmer to hexamer.
The transformation consists of a 6 Å axial shift
accompanied by an 11.4° counter-clockwise rotation about an
axis parallel to the molecular 6-fold axis, resulting in
relative preservation of the interdomain interface.
(C)
Representative electron density of 14-fold averaged D2 domain.
(D) The conformation of the nucleotide binding site of D2
fragment is shown with characteristic AAA motifs highlighted as
follows: Walker A (slate); Walker B (red); sensor 1 (purple);
sensor 2 (purple); arginine finger (white); N-linker (pink).
(E) The D2 binding sites of the full-length models are
superposed for the ATP (magenta), ADP-AlF[x] (blue), and ADP
(green) state with ADP shown bound in the pocket.
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