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PDBsum entry 2bke
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DNA binding protein
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PDB id
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2bke
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References listed in PDB file
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Key reference
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Title
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Conformational flexibility revealed by the crystal structure of a crenarchaeal rada.
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Authors
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A.Ariza,
D.J.Richard,
M.F.White,
C.S.Bond.
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Ref.
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Nucleic Acids Res, 2005,
33,
1465-1473.
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PubMed id
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Abstract
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Homologous recombinational repair is an essential mechanism for repair of
double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial
role in this process, forming filaments that utilize ATP to mediate their
interactions with single- and double-stranded DNA. The recombinase molecules
present in the archaea (RadA) and eukaryota (Rad51) are more closely related to
each other than to their bacterial counterpart (RecA) and, as a result, RadA
makes a suitable model for the eukaryotic system. The crystal structure of
Sulfolobus solfataricus RadA has been solved to a resolution of 3.2 A in the
absence of nucleotide analogues or DNA, revealing a narrow filamentous assembly
with three molecules per helical turn. As observed in other RecA-family
recombinases, each RadA molecule in the filament is linked to its neighbour via
interactions of a short beta-strand with the neighbouring ATPase domain.
However, despite apparent flexibility between domains, comparison with other
structures indicates conservation of a number of key interactions that introduce
rigidity to the system, allowing allosteric control of the filament by
interaction with ATP. Additional analysis reveals that the interaction
specificity of the five human Rad51 paralogues can be predicted using a simple
model based on the RadA structure.
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Figure 2.
The oligomerization strand. (a)
{sigma} ; purple mesh) of the region surrounding Phe73. Atoms from different monomers
are coloured differently (grey/blue). (b) A cluster of salt bridges stabilizes the SsRadA
oligomerization motif. (c) Superposition of the oligomerization strands of SsRadA (blue),
EcRecA (green) and HsRad51/BRCA2 (magenta). The common ATPase domain of the interacting
subunit is shown as a grey surface. (d and e) Conserved interactions between the
N-terminal domain of SsRadA, MvRadA and ScRad51, with the neighbouring ATPase domain.
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Figure 3.
Interactions between ATPase subunits for SsRadA (blue), ScRad51 (red) and
PfRadA (green). Structures were superimposed on one subunit (shown as backbone trace). The
neighbouring subunits are shown as semi-transparent surfaces, with a solid cartoon
representation of residues between helices {alpha} 10 and {alpha} 12. (a) Side
view. (b) Top view.
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The above figures are
reprinted
from an Open Access publication published by Oxford University Press:
Nucleic Acids Res
(2005,
33,
1465-1473)
copyright 2005.
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