Figure 5.
FIG. 5. Comparisons of cysteinylated and free cysteine
residues on a PriB dimer. Cys-12 (C12) and Cys-27 (C27) of
monomer A (designated by the letter A in parentheses) are shown
in panels A and B, respectively. Cys-12 and Cys-27 of monomer B
(designated by the letter B in parentheses) are shown in panels
C and D, respectively, for comparison. Cysteinyl moieties are
shown as ball-and-stick models, whereas residues surrounding
those cysteinyl moieties are shown as stick models and labeled
using single letter amino acid abbreviations with position
numbers. The electron
density maps contoured at 1 show cysteinylated
cysteines as orange mesh. The coordinating waters are presented
as cyan balls. The disulfide bonds are shown as yellow dotted
lines, and the hydrogen bonds are shown as brown dotted lines.
In panel D, which shows the free Cys-27 of monomer B, a stick
model of Cys-27 of monomer A is presented in brown as a
comparison.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
50465-50471)
copyright 2004.
electron
density maps contoured at 1 
show cysteinylated
cysteines as orange mesh. The coordinating waters are presented
as cyan balls. The disulfide bonds are shown as yellow dotted
lines, and the hydrogen bonds are shown as brown dotted lines.
In panel D, which shows the free Cys-27 of monomer B, a stick
model of Cys-27 of monomer A is presented in brown as a
comparison.