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Figure 2.
Figure 2. HtrA2/Omi forms a pyramid-shaped homotrimer. a, The
HtrA2/Omi trimer is viewed either along (left) or perpendicular
to (right) the three-fold symmetry axis. Trimerization is
mediated exclusively by the serine protease domain. The
N-terminal IAP-binding tetrapeptide motif is located at the top
of the pyramid, and the PDZ domain is at the base. b, Surface
representation of the HtrA2/Omi structure. White arrows indicate
the positions of the catalytic Ser residues. c, A slice of
HtrA2/Omi structure to highlight the position of the catalytic
residue. The HtrA2/Omi surface is represented by color-coded
mesh, with the same scheme as in (a,b) and an orientation
similar to that in (a, right). d, A stereo view of part of the
trimerization interface. The three HtrA2/Omi monomers are
colored green, orange and blue, with their side chains in red.
Three aromatic residues from each monomer interdigitate to form
a tighly packed hydrophobic interface. The experimental electron
density, contoured at 1.5  ,
is shown in green around the three aromatic residues.
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