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Figure 1.
Figure 1. Crystal Structure of p97 N D1 Domain(A) Ribbon
representation of N D1 protomer structure. The domains are
colored individually, with the N-terminal double ψ barrel
domain (yellow), β barrel domain (gold), the D1 α/β domain
(cyan), and the C-terminal α-helical domain (blue). Also
highlighted are the Walker A (P loop) motif (black), Walker B
(DExx box) motif (mauve), sensor loop (red), and the proposed
hinge region between the N and D1 domains (magenta). Bound ADP
nucleotide is shown as balls and sticks. For clarity, only the
secondary structure elements discussed in the text are
labeled.(B) A close-up view of the N D1 interface (boxed region
in [A]). A small rotation was applied to optimize the view of
the interface.(C) The N D1 hexamer forms a wheel-like structure
of  vert,
similar 160 Å in diameter and a central hole vert,
similar 15 Å in diameter. One protomer is colored as in
(A). The α/β domain fold (cyan) forms the spokes of the wheel,
while the helical domain (blue) forms the outer rim. N-terminal
domains (yellow) are oriented counterclockwise off the main body
of the wheel. Bound ADP moieties (brown) drawn as Van der Waal
spheres are located between protomers. The arrow indicates the
ADP binding pocket.(D) The N D1 hexamer is rotated 90°
(relative to Figure 1C) so that the amino-terminal side is on
top. The thickness of N D1 is vert,
similar 20–40 Å. The N domain lies in the same plane as
D1 and spans a similar thickness. Note the ADP moieties (brown
spheres) bound in deep pockets.(E) A close-up view of the
hexamer interface (boxed in [C]). For clarity, only secondary
structure elements discussed in the text are labeled. The dashed
line indicates the protomer–protomer interface. The sensor
residues (Asn-348, yellow; Arg-359, blue) are shown as sticks
near the interface.
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