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Figure 7.
Fig. 7. Stereo views of the three-dimensional structures of
the propeptide:subtilisin complexes. (a) The entire structure of
the G56S-propeptide:S324A-subtilisin complex is superimposed on
that of the Tk-propeptide:S324A-subtilisin complex (Protein Data
Bank code 2Z30). For the structure of the
G56S-propeptide:S324A-subtilisin complex, G56S-propeptide is in
red and S324A-subtilisin is in green. Two active-site residues
(Asp115 and His153) and Ala324, which is substituted for the
active-site serine residue, are indicated by yellow stick
models, in which the oxygen and nitrogen atoms are in red and
blue, respectively. Seven Ca^2 + are shown in cyan spheres. N
and C represent the N- and C-termini, respectively. The entire
structure of the Tk-propeptide:S324A-subtilisin complex,
including seven Ca^2 +, is in gray. (b–d) G56S-propeptide (b),
G56E-propeptide (c), and G56W-propeptide (d) in the structures
of the G56S-propeptide:S324A-subtilisin,
G56E-propeptide:S324A-subtilisin, and
G56W-propeptide:S324A-subtilisin complexes are superimposed on
Tk-propeptide in the structure of the
Tk-propeptide:S324A-subtilisin complex. The view direction is
changed from (a), such that the mature domain is located behind
the propeptide. The mutant and wild-type propeptides are in red
and gray, respectively. Nine of the 11 residues that form a
hydrophobic core and Ser56 (b), Glu56 (c), or Trp56 (d) are
indicated by blue and yellow stick models, respectively. Two
other core-forming residues are not shown because they are
hidden.
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