Figure 2.
Fig. 2. Stereo-views of the acyl-enzyme complex formed
between N-acetyl-Val-Glu-Pro-Ile-CO[2]H (in gold) and PPE (in
green). The peptide is linked via an ester bond between its
C-terminal isoleucine and Ser195 of PPE. (A) Location of the
proposed hydrolytic water molecule (Wat532) hydrogen bonded to
N[ 2] of His57
and poised for nucleophilic attack above the ester carbonyl. (B)
Antiparallel sheet formed
between N-acetyl-Val-Glu-Pro-Ile-CO[2]H and the Ser214–Val216
loop in the active site of PPE. The 2mF[o]DF[c] electron density
maps [26] were contoured at 1 . This figure
was produced using BOBSCRIPT [27], RASTER3D [28], IMAGEMAGICK
and PHOTOSHOP 5.0 (Adobe Systems Inc.).
The above figure is reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2001,
268,
2969-2974)
copyright 2001.
2] of His57
and poised for nucleophilic attack above the ester carbonyl. (B)
Antiparallel 
sheet formed
between N-acetyl-Val-Glu-Pro-Ile-CO[2]H and the Ser214–Val216
loop in the active site of PPE. The 2mF[o]DF[c] electron density
maps [26] were contoured at 1 
. This figure
was produced using BOBSCRIPT [27], RASTER3D [28], IMAGEMAGICK
and PHOTOSHOP 5.0 (Adobe Systems Inc.).