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Figure 1.
FIG. 1. The structures of Hp ClpX-ASD, E. coli HslU, and E.
coli ClpA D2. A, the overall structure of Hp ClpX-ASD is
presented as a ribbon diagram. The ATPase core domain, SSD
domain, and LGF tripeptide are colored magenta, green, and red,
respectively. The ATP molecule is shown in orange as a
ball-and-stick model. Each secondary structure and the N and C
termini are labeled. The protease interface and substrate
interface are indicated in the figure to display the relative
orientation of Hp ClpX. E. coli HslU (B) and E. coli ClpA D2
(C), positioned in the same orientation with Hp ClpX-ASD, are
displayed as ribbon diagrams, with the same color codes. D, the
sequences of Hp ClpX, E. coli ClpX, and E. coli HslU were
aligned by the CLUSTALW program (28), following the manual
adjustment based on a structural comparison. The secondary
structures of Hp ClpX-ASD are indicated by a cylinder for the
 -helix and an arrow for
the  -strand. The amino acids
in the LGF peptide are boxed in blue. In the alignment,
identical residues are boxed in red, with homologous residues
boxed in yellow.
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