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Figure 2.
Fig. 2. Ribbon diagrams of PhzF in the open and closed
forms, substrate binding to the active site, and comparison to
the active sites of related proteins. Overall structure of PhzF
in the open (A) and closed (B) forms. Binding partners are
sulfate (A) and 3OHAA (B). Key building blocks of the C-terminal
domain in one monomer are color-coded: green, central  -helix;
blue, eight-stranded  -barrel; and red,
decorating -helices. Secondary
structure is labeled in the other monomer. The surface in B
demonstrates the size of the intermonomer cavity in the closed
form. (C) Stereoview of DHHA binding to the active site of PhzF.
The proposed position of E45 in reprotonation is shown in red.
Conserved residues are shown in magenta, and the positions of
the catalytic cysteines in DapF are shown in cyan. (D) Active
sites of DapF (Left), YddE (Center), and phenazine-biosynthesis
protein from Enterococcus faecalis V583 (Right). All structures
were prepared with BOBSCRIPT (32).
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