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Figure 1.
Solution NMR structures of SelM and Sep15. A, backbone
superposition of the 20 lowest energy structures of SelM (left
panel) and Sep15 (right panel). B, ribbon representation of the
SelM (left panel) and Sep15 (right panel) structures that are
closest to the mean with α-helices colored blue (α1-α3),
β-strands colored orange (β1-β4), and coils colored gray. The
locations of the redox-active motifs for SelM (CXXU) and Sep15
(CXU) are indicated. Residues 25-34 and residues 121-145
(including an uncleaved C-terminal hexahistidine tag) of SelM
are not shown because these regions are flexible. Residues 62-70
(including an uncleaved N-terminal hexahistidine tag) and
residues 150-178 of Sep15 are not shown because these regions
are also flexible. This figure was prepared with MOLMOL and
PyMOL (52).
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