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Figure 2.
Figure 2. Monomeric structures of a, CesT and b, SigE. c,
Structure-based sequence alignment of CesT (top) and SigE
(bottom). Helices are shaded blue; strands, green. Hydrophobic
residues exposed on the surface of the SigE or SigE-like CesT
homodimers are highlighted in red. The C-terminal amphipathic
helix predicted by sequence analysis to be a potential source of
hydrophobic residues for interaction with effector proteins4
packs with its hydrophobic face pointing into the buried
hydrophobic core of the protein in both CesT and SigE. Thus,
this region unlikely provides interactions with the effector
unless dramatic unfolding of the chaperone occurs upon complex
formation. (a,b), as well as Fig. 3a -c, were generated by
MOLSCRIPT34 and RASTER3D^35.
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