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Figure 3.
Figure 3. Overall Structure of PCS Complexed with CoA-SH
(A) Ribbon representation of the PCS homodimer. The monomers are
colored green and silver, and the CoA-SH molecules are shown as
blue stick models. The catalytic Cys174 and Met147, which form a
partial wall of the active-site cavity of another monomer, are
highlighted as yellow CPK and stick models, respectively.
(B) Comparison of PCS (green), M. sativa CHS (blue), and G.
hybrida 2PS (purple). The catalytic Cys174 and the bound CoA-SH
in PCS are also shown as yellow and red CPK molecules,
respectively.
(C) CoA-SH binding to the PCS structure. The
CoA-SH (green) and the SIGMA-weighted |2F[o] − F[c]| electron
density (0.8σ, red cage) for CoA-SH are shown. The water
molecules (light-blue spheres) and hydrogen bonds (dotted lines)
are also indicated.
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