Figure 4.
Fig. 4. Initiator AAA+ interactions. (A) The AAA+ domains of
ATP-bound DnaA (Aquifex aeolicas, Protein Data Bank accession
number 2HCB) (24) assemble in a head-to-tail oligomer that
places the arginine finger of the box VII helix (gold) into the
ATPase active site of the adjacent protomer. (B) Stereo view of
the Orc1-1/Orc1-3 DNA complex
shows that contacts between adenosine diphosphate–bound
initiators and DNA orient successive AAA+ domains into a
similar, albeit more open, configuration to that of oligomerized
DnaA. For clarity, only initiator AAA+ domains are shown in (A)
and (B). Bound nucleotides (black) and magnesium ions (magenta)
are shown as spheres.
The above figure is reprinted
by permission from the AAAs:
Science
(2007,
317,
1210-1213)
copyright 2007.
DNA complex
shows that contacts between adenosine diphosphate–bound
initiators and DNA orient successive AAA+ domains into a
similar, albeit more open, configuration to that of oligomerized
DnaA. For clarity, only initiator AAA+ domains are shown in (A)
and (B). Bound nucleotides (black) and magnesium ions (magenta)
are shown as spheres.