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Figure 3.
Figure 3. Crystal Structure of the C44 Tetramer
(A)
Lateral view of the C44 tetramer. Yellow van der Waals surfaces
identify residues at the a positions, red surfaces identify
residues at the d positions, and light-blue surfaces identify
residues at the g positions. The N termini of helices A and B
are indicated.
(B) Axial view of the C44 tetramer. The red
van der Waals surfaces of the Ile1154(d) and Leu1182(d) side
chains are depicted.
(C) Cross-section of the tetramer in
the Ile1161(d) layer. The 1.70 Å 2F[o] − F[c] electron
density map (contoured at 1.2σ) is shown with the refined
molecular model.
(D) Helical wheel representation of
residues 1153–1185 of the C44 tetramer. Heptad-repeat
positions are labeled a–g. The C44 helices interact through a
previously uncharacterized type of packing interaction between
the a, d, and g side chains (colored green). Figure 3.
Crystal Structure of the C44 Tetramer(A) Lateral view of the C44
tetramer. Yellow van der Waals surfaces identify residues at the
a positions, red surfaces identify residues at the d positions,
and light-blue surfaces identify residues at the g positions.
The N termini of helices A and B are indicated.(B) Axial view of
the C44 tetramer. The red van der Waals surfaces of the
Ile1154(d) and Leu1182(d) side chains are depicted.(C)
Cross-section of the tetramer in the Ile1161(d) layer. The 1.70
Å 2F[o] − F[c] electron density map (contoured at 1.2σ)
is shown with the refined molecular model.(D) Helical wheel
representation of residues 1153–1185 of the C44 tetramer.
Heptad-repeat positions are labeled a–g. The C44 helices
interact through a previously uncharacterized type of packing
interaction between the a, d, and g side chains (colored green).
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