Figure 1.
Figure 1. Biological and structural analysis of EstE7. (a)
Relative activity of recombinant EstE7 toward p-nitrophenyl
esters. Esterase activity was determined photometrically in a 50
mM Tris-HCl buffer (pH 7.5) using various p-nitrophenyl esters
as substrates. (b) The EstE7 monomer structure has two domains:
an /
domain
(green) and a regulatory domain (blue). The catalytic triad
residues are shown in ball-and-stick representations. (c)
Nucleophile Ser157 in molecule A interact with -mercaptoethanol.
The catalytic site consists of three residues: Ser157
(nucleophile), Glu251 (charge-relay network), and His281 (proton
carrier). -mercaptoethanol
is shown in ball-and-stick representations. A
weighted electron density maps (2Fo - Fc) contoured at 1 in
the vicinity of catalytic residues and -mercaptoethanol.
(d) Substrate-binding tunnel. This tunnel of the hydrophobic
pocket has an ovoidal shape with approximate depth of 16
Å. The nucleophile Ser157 residue is shown in
ball-and-stick representations in the area of the orange dotted
circle.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
1036-1040)
copyright 2009.
/
domain
(green) and a regulatory domain (blue). The catalytic triad
residues are shown in ball-and-stick representations. (c)
Nucleophile Ser157 in molecule A interact with 
A
weighted electron density maps (2Fo - Fc) contoured at 1 
16
Å. The nucleophile Ser157 residue is shown in
ball-and-stick representations in the area of the orange dotted
circle.