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Figure 2.
Fig. 2. Complexes of ZnCcP with various Cc mutants have
different association modes. (A) Representative ribbon diagrams
for ZnCcP bound to Cc variants. From left to right: yCc WT,
F82W, and F82S mutants; yCc F82Y and F82I mutants; horse Cc; yCc
K72S/F82Y. (B) Relative positioning and interface structures for
the ZnCcP:F82W yCc (Left) and ZnCcP:yCc F82I (Right) complexes.
Cc (gray ribbons, top) rotates 90° and
translates8Åinthe F82I mutant generating altered heme
orientations (yellow bonds), interprotein contacts (black and
orange side chains), and intervening solvent structure (red
spheres) with CcP (yellow, below) compared with the F82W
complex. (C) Superposition of ZnCcP from the two ZnCcP: F82S yCc
complexes (red and blue) indicate variability in Cc positioning
within the asymmetric unit.
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