Figure 4.
Figure 4 Active site of PriA. (A) Superimposition of the active
sites of PriA (blue) and HisA (green). Active-site residues and
the two bound sulphate ions are shown in stick mode. The carbon
atoms are in the colour of the corresponding C[ ]trace.
Oxygen molecules are coloured red and sulphur in yellow. (B)
Superimposition of the active sites of PriA (blue) and TrpF
(black). Active-site residues and the two bound sulphate ions
are shown in stick mode using atom-type colours. (C) PriA active
sites with the HisA product analogue rPRFAR. The rPRFAR
coordinates have been taken from the superimposed HisF structure
(not shown) in the presence of rPRFAR (Chaudhuri et al, 2001).
Residues most probably involved in catalysis are highlighted
green, surrounded by red circles, in this panel and in all
following panels with modelled complexes. (D) PriA active site
with the TrpF product analogue rCdRP. The rCdRP coordinates were
obtained from the superimposed TrpF structure in complex with
rCdRP (Henn-Sax et al, 2002). (E) PriA active site with the TrpF
product analogue rCdRP modelled binding to the second phosphate
binding site. The rCdRP coordinates were obtained from the TrpF
structure in complex with rCdRP (Henn-Sax et al, 2002)
superimposed with the C-terminal half-barrel of PriA. Complete
PriA was then superimposed using the coordinates obtained from
the C-terminal half-barrel. (A -E) Prepared with DINO
(http://www.dino3d.org) and rendered with POVRAY 3.6
(http://www.povray.org).
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO Rep
(2005,
6,
134-139)
copyright 2005.
]trace.
Oxygen molecules are coloured red and sulphur in yellow. (B)
Superimposition of the active sites of PriA (blue) and TrpF
(black). Active-site residues and the two bound sulphate ions
are shown in stick mode using atom-type colours. (C) PriA active
sites with the HisA product analogue rPRFAR. The rPRFAR
coordinates have been taken from the superimposed HisF structure
(not shown) in the presence of rPRFAR (Chaudhuri et al, 2001).
Residues most probably involved in catalysis are highlighted
green, surrounded by red circles, in this panel and in all
following panels with modelled complexes. (D) PriA active site
with the TrpF product analogue rCdRP. The rCdRP coordinates were
obtained from the superimposed TrpF structure in complex with
rCdRP (Henn-Sax et al, 2002). (E) PriA active site with the TrpF
product analogue rCdRP modelled binding to the second phosphate
binding site. The rCdRP coordinates were obtained from the TrpF
structure in complex with rCdRP (Henn-Sax et al, 2002)
superimposed with the C-terminal half-barrel of PriA. Complete
PriA was then superimposed using the coordinates obtained from
the C-terminal half-barrel. (A -E) Prepared with DINO
(http://www.dino3d.org) and rendered with POVRAY 3.6
(http://www.povray.org).