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Figure 1.
Fig. 1. Structural overview of SOR. The x-ray structure of the
SOR-E114A homodimer in the native reduced state is shown as
magenta (monomer A) and cyan (monomer B) ribbons with the
exception of the LID loop (residues 45 to 49), which is colored
in dark green and orange for monomers A and B, respectively.
Reduced and oxidized iron atoms are shown as green and orange
balls, respectively. (Inset) The active site of monomer B upon
addition of H[2]O[2]. The residues coordinating the active iron
(His^49, His^69, His^75, His^119, and Cys^116) as well as Lys^48
are represented as sticks. The bound peroxide ligand is shown as
a red stick. Water molecules are shown as red balls. In order to
support the diatomic nature of the peroxide intermediate,
simulated annealed F[obs] – F[calc] maps omitting the distal
or proximal oxygens of the O-O moiety, respectively, were
calculated. The two maps are displayed in green (distal) and
orange (proximal) at a contour level of 3.0  .
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