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Figure 2.
FIG. 2. A stereo view of the CerHb heme distal (upper part
of the figure) and proximal sites (lower part, hosting His-F8).
Short fragments of the B- and E-helices are displayed as cyan
ribbons. The heme is shown in red. The relevant residues are
displayed with light gray bonds, using black labels for the
wild-type CerHb structure. Structural modifications observed in
the Thr-E11  Val CerHb mutant are
highlighted by displaying residues Tyr-B10 and Val E11
in orange. The dashed arrows indicate hydrogen bond donation in
the wild-type protein (blue arrows) and in the Thr-E11 Val
mutant (orange arrow). The O[2] molecule is displayed at the
sixth coordination site of the heme iron as a purple diatomic
species (partly covered by arrows). Lys-E10 is electrostatically
coupled to both heme propionates and contributes to the
shielding of the distal heme pocket.
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