|
Figure 4.
A, overall structure of the C. symbiosum GcdA monomer. α-
and 3[10]-helices of the N-terminal domain are colored blue, the
respective β-strands are shown in lighter blue. The secondary
structure motifs of the C-terminal domain are represented in
dark green (helices) and light green (β-strands). The bound
crotonyl-CoA is displayed as a magenta stick model and the
chloride ion bound to OAH2 is shown as a yellow sphere. Residues
missing in the electron density are indicated by broken lines.
B, GcdA dimer. N and C terminus of the symmetry-equivalent chain
B are colored dark and light gray, respectively. The
crotonyl-CoA molecules at the dimer interfaces are represented
as CPK models. The second chloride ion is displayed as a green
sphere. The positions of the active sites are highlighted by
dashed lines. C, two orthogonal orientations of the
222-symmetric GcdA tetramer deduced from the crystal packing.
Chains A to D are colored blue, green, red, and yellow,
respectively.
|
