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Figure 1.
Fig. 1. Structure of DsbG. (a) Crystal structure of the
DsbG homodimer. (b) Each DsbG monomer consists of an N-terminal
dimerization domain (blue), a linker helix (gray), and a
C-terminal catalytic domain that has a TRX fold (pink). The
active-site disulfide is shown in green. (c) Interaction between
the two V-shaped DsbG homodimers (blue and gray) found in the
crystal structure. The asymmetric unit contains one blue subunit
and one gray subunit. The biological dimer (two blue or two gray
subunits) is generated by applying crystallographic symmetry, as
indicated by an arrow. (d) Stereoview of interactions with the
Cys at the active site of reduced DsbG (synchrotron data).
Figures were generated with MOLSCRIPT (32).
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