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Figure 1.
The Gfh1 structure and comparison with GreA and DksA. A,
alignment of the Gfh1 and GreA sequences. The residues with
conserved chemical properties among Gfh1 and GreA sequences that
might thus form the Gfh1-like (hydrophobic) and GreA-like
(”polar“) interface in both protein families are marked with
yellow and green boxes, respectively, whereas the unfavorable
substitutions in both Gfh1 and GreA are outlined by red boxes.
The potentially functionally crucial segments at the tip of the
CC-domains are highlighted with magenta. B, the structure of the
Gfh1 protein. The acidic side chains at the CC tip are shown in
red. C, the Gfh1 and GreA structures superimposed by the
G-domains. D, the CC tips of DksA (green), GreA (yellow), and
Gfh1 (cyan). DksA and GreA are superimposed by the CC-domains,
and the Gfh1 CC tip is shown in a similar orientation. The
hydrogen bonds stabilizing the α-turns in GreA, and DksA are
shown as white dashed lines.
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