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PDBsum entry 2chv
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DNA binding protein
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PDB id
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2chv
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References listed in PDB file
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Key reference
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Title
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Communication between subunits within an archaeal clamp-Loader complex.
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Authors
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A.Seybert,
M.R.Singleton,
N.Cook,
D.R.Hall,
D.B.Wigley.
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Ref.
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EMBO J, 2006,
25,
2209-2218.
[DOI no: ]
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PubMed id
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Abstract
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We have investigated the communication between subunits in replication factor C
(RFC) from Archaeoglobus fulgidus. Mutation of the proposed arginine finger in
the small subunits results in a complex that can still bind ATP but has impaired
clamp-loading activity, a process that normally only requires binding of
nucleotide. The small subunit alone forms a hexameric ring that is six-fold
symmetric in the absence of ATP. However, this symmetry is broken when the
nucleotide is bound to the complex. A conformational change associated with
nucleotide binding may relate to the opening of PCNA rings by RFC during the
loading reaction. The structures also reveal the importance of the N-terminal
helix of each subunit at the ATP-binding site. Analysis of mutant protein
complexes containing subunits lacking this N-terminal helix reveals key distinct
regulatory roles during clamp loading that are different for the large and small
subunits in the RFC complex.
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Figure 2.
Figure 2 Overall fold of a monomer of the A. fulgidus RFC small
subunit. The N-terminal domain 1 is coloured in red, domain 2 is
blue and domain 3 is green. The inset shows a zoom in the
ATP-binding site, with difference (F[o]-F[c]) electron density
for one of the ADPNP molecules bound to the complex.
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Figure 5.
Figure 5 (A) The location of the N-terminal helix (RFC box II)
within the ATP-binding site. (B) Diagram showing how the
N-terminal helix blocks access of the arginine finger (Arg152)
to the ATP-binding site.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2006,
25,
2209-2218)
copyright 2006.
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