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Figure 3.
Fig. 3. Overview of HMGS in complex with F-244. (A)
Electrostatic surface of HMGS covalently bound to ring-opened
F-244. Color-coding is identical to Fig. 2A. The inhibitor F-244
does not occupy the same part of the pantothenate-binding tunnel
as the CoA tail shown in Fig. 2A. (B) Stereoview of the HMGS
active site for the ring-opened F-244 covalent complex.
Color-coding and map calculations are identical to Fig. 2B. The
first eight carbons of the acyl tail of F-244 are well ordered;
however, the position of the remaining six carbons display much
weaker electron density as the tail protrudes out of the active
site entrance. (C) Close-up view of the HMGS active site for the
ring-opened F-244 covalent complex. The SIGMAA-weighted 2F[o] -
F[c] electron density map is shown in blue, contoured at 1  . A
H-bond between Glu-83 and the 2-hydroxymethyl moiety of
ring-opened F-244 is shown as rendered green cylinders.
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