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Figure 1.
Figure 1. Structure of HtrA2/Omi. a, Schematic representation
of the HtrA2/Omi monomer. The serine protease and the PDZ
domains are colored cyan and pink, respectively. The flexible
linker between the two domains is represented by a dotted line.
The position of the catalytic Ser 306 is highlighted in red. b,
A close-up view of the intramolecular hydrophobic contacts
between the protease and the PDZ domains. Residues from the
protease and the PDZ domains are shown in yellow and orange,
respectively. c, Superposition of the PDZ domains from HtrA2/Omi
(pink) and the membrane-associated protein syntrophin (green,
PDB entry 2PDZ)31. Strands  5/
6
from the serine protease domain and the syntrophin-bound peptide
are shown in cyan and dark blue, respectively. d, Sequence
alignment of the human HtrA proteins and their homolog in E.
coli. The alignment was generated by ClustalW32. The secondary
structural elements are indicated above the alignment. The
catalytic triad residues are boxed in red, and regions critical
for homotrimerization or intramolecular contacts are indicated
below the alignment. Conserved residues are boxed in yellow.
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