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Figure 1.
The M. barkeri α[2]ε[2] Ni-CODH component, subunits, and
cofactors. (A) Side view of the α[2]ε[2] component. The
protein is shown as ribbons with the α-subunits colored in cyan
and green and the ε-subunits in tan and orange. The atoms of
the metal clusters are shown as spheres, with Fe atoms colored
in purple, Ni atoms in blue, and the remaining atoms in CPK. (B)
Side view of metal clusters in the α[2]ε[2] complex. (C) Top
view of the α[2]ε[2] component. (D) Top view of the right
α-subunit highlighting its different domains. The ε-subunit is
omitted. The α-subunit is colored in rainbow by domain:
N-terminal portion (magenta), N-terminal α-helical domain
(blue), first Rossmann-like domain (cyan), FeS-binding domain
(green), second C-cluster Rossmann-like domain (yellow), and
C-terminal domain (orange). The β-hairpin insert in the second
Rossmann-like domain is colored in red. (E) Ribbon diagram of
ε-subunit colored by secondary structure with α-helices in
tan, β-sheets in magenta, and loops in cyan. The orientation of
this subunit matches the ε-subunit shown as tan surface in F.
(F) Docking interaction between the α- and ε-subunits colored
as in A. The left ε-subunit is shown as a surface with an FAD
molecule shown and colored in CPK to illustrate its fit to the
cavity. No FAD was observed in the α[2]ε[2] structure. The
β-strands in the right ε-subunit are colored in marine for
better visualization.
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