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Figure 4.
Figure 4 Interactions of the two DsbC active sites with DsbD
 residues.
(A) Stereo diagram of the primary binding site showing the DsbC
active site interacting with DsbD .
The primary binding surface of DsbD is
shown colored according to the calculated electrostatic
potential using GRASP. Negative charges are colored red and
positive charges are in blue. Important DsbC residues
(Ile96−Leu104, Gly181−Val185) are shown in blue
ball-and-stick and cartoon representation. DsbC residues are
labeled in black and DsbD residues
in green. DsbC Tyr100 binds into an uncharged pocket adjacent to
the DsbD active
site Cys109, which forms a disulfide bond with DsbC Cys98 and
hydrogen bonds to the cis-proline loop, Thr182−Pro183. (B)
Stereo diagram of the secondary binding site. The electrostatic
surface of the DsbD secondary
binding site is presented with DsbD residues
labeled in green. The DsbC active region is shown in green
ball-and-stick and ribbons representation with yellow labels.
DsbD Asp21
interacts with the DsbC active site Cys98 and Gly99, while
Tyr100 packs against DsbD Phe22.
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