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PDBsum entry 1z8s
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References listed in PDB file
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Key reference
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Title
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Solution structure of the helicase-Interaction domain of the primase dnag: a model for helicase activation.
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Authors
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K.Syson,
J.Thirlway,
A.M.Hounslow,
P.Soultanas,
J.P.Waltho.
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Ref.
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Structure, 2005,
13,
609-616.
[DOI no: ]
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PubMed id
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Abstract
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The helicase-primase interaction is a critical event in DNA replication and is
mediated by a putative helicase-interaction domain within the primase. The
solution structure of the helicase-interaction domain of DnaG reveals that it is
made up of two independent subdomains: an N-terminal six-helix module and a
C-terminal two-helix module that contains the residues of the primase previously
identified as important in the interaction with the helicase. We show that the
two-helix module alone is sufficient for strong binding between the primase and
the helicase but fails to activate the helicase; both subdomains are required
for helicase activation. The six-helix module of the primase has only one close
structural homolog, the N-terminal domain of the corresponding helicase. This
surprising structural relationship, coupled with the differences in surface
properties of the two molecules, suggests how the helicase-interaction domain
may perturb the structure of the helicase and lead to activation.
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Figure 6.
Figure 6. A Model for the DnaB-P16 Interaction
(A) The
3-fold symmetric ring of hexameric DnaB, showing the N-domain of
one monomer (6N) interacting with the C-domain (5H) of the
neighboring monomer (Yang et al., 2003).
(B) In the
DnaB-P16 complex, the P16 protein (shaded purple) interacts with
the linker region that connects the N-terminal (6N) and
C-terminal (6H) domains of one monomer, via its C2 subdomain. In
addition, the C1 subdomain displaces 6N while at the same time
maintaining the interactions with 5H that are essential to
preserve a 3-fold symmetric ring in the helicase-primase complex.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
609-616)
copyright 2005.
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