Figure 5.
Figure 5. Conformational changes induced by ATP binding. (a)
ATP-DnaA dimer (blue and gold) with ADP-DnaA (green; PDB entry
1L8Q) superposed on one subunit. (b) Detail, with arrows
indicating movement of the AAA+ lid (DnaA domain IIIB) required
to accommodate a steric clash that occurs in the ADP-DnaA AAA+
orientation (red circle). (c) Stereo view of the molecular
features of the ADP-to-ATP switch. The lid movement is
stabilized by interactions of the sensor II (SII) arginine with
the -phosphate
and enables the box VII helix to engage the nucleotide through
the arginine finger (Arg230). Further stability is provided by
interactions of Glu280 with the ribose ring and of the box VII
residue Ser229 with Arg277.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2006,
13,
676-683)
copyright 2006.
-phosphate
and enables the box VII helix to engage the nucleotide through
the arginine finger (Arg230). Further stability is provided by
interactions of Glu280 with the ribose ring and of the box VII
residue Ser229 with Arg277.