Figure 6.
Figure 6 Molecular-surface representation of SoxS. (a)
Representation of the molecular surface coloured according to
the electrostatic potential. The yellow asterisk indicates the
position of the redox-active Cys13. The molecular surface is
coloured according to the electrostatic potential as calculated
with the program APBS (Baker et al., 2001[Baker, N. A., Sept,
D., Joseph, S., Holst, M. J. & McCammon, J. A. (2001). Proc.
Natl Acad. Sci. USA, 98, 10037-10041.]). The molecular surface
is colour-ramped according to the electrostatic potential, with
red indicating negative potential and blue indicating positive
potential; fully saturated colours indicate a potential of or
equal to] ±4kT/e (assuming an ionic strength of 150 mM, a
protein interior dielectric of 2 and a solvent dielectric of
78.5). The rendered surface representation was prepared with
PyMOL (DeLano, 2004[DeLano, W. L. (2004). The PyMOL Molecular
Graphics System. http://www.pymol.org .]). (b) The putative
binding cleft on the surface of SoxS. The spheres are coloured
according to the type of the underlying atom (carbon, green;
nitrogen, blue; oxygen, red; sulfur, yellow). For the putative
substrate-binding epitope the C atoms are coloured magenta. The
S atom of the redox-active cysteinyl residue Cys13 is labelled
as well as the aromatic amino-acid residues located at the
surface near the active site.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2009,
65,
229-240)
copyright 2009.
or
equal to] ±4kT/e (assuming an ionic strength of 150 mM, a
protein interior dielectric of 2 and a solvent dielectric of
78.5). The rendered surface representation was prepared with
PyMOL (DeLano, 2004[DeLano, W. L. (2004). The PyMOL Molecular
Graphics System. http://www.pymol.org .]). (b) The putative
binding cleft on the surface of SoxS. The spheres are coloured
according to the type of the underlying atom (carbon, green;
nitrogen, blue; oxygen, red; sulfur, yellow). For the putative
substrate-binding epitope the C atoms are coloured magenta. The
S atom of the redox-active cysteinyl residue Cys13 is labelled
as well as the aromatic amino-acid residues located at the
surface near the active site.