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Figure 3.
Fig. 3. (a) The topology of RLuc8's α/β-hydrolase fold
domain. α-Helices are shown in blue, and β-sheets are shown in
red. Numbering/lettering of the sheets/helices is done with
respect to the standard for α/β-hydrolases,^33 and the
locations of the presumptive catalytic residues are marked. The
cap domain is an excursion from the fold pattern composed of
residues 146–230 in the luciferase. (b) The domains of RLuc8.
Shown are the locations of the cap domain (in gray) and
α/β-hydrolase fold domain (blue to red) in the context of the
crystal structure. (c) Close-up stereo cartoon representation of
the active site of the RLuc8:diammonium structure. The
presumptive active site residues are color coded with respect to
the average degree of enzymatic perturbation mutagenesis at the
site yields, based on published data.^22^,^23 Mutations at
green-, yellow-, and orange-colored residues were associated
with <1%, 1–10%, and 10–100%, respectively, of full
enzymatic activity.
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