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PDBsum entry 1pzn
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Recombination
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PDB id
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1pzn
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Contents |
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300 a.a.
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(+ 0 more)
239 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Full-Length archaeal rad51 structure and mutants: mechanisms for rad51 assembly and control by brca2.
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Authors
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D.S.Shin,
L.Pellegrini,
D.S.Daniels,
B.Yelent,
L.Craig,
D.Bates,
D.S.Yu,
M.K.Shivji,
C.Hitomi,
A.S.Arvai,
N.Volkmann,
H.Tsuruta,
T.L.Blundell,
A.R.Venkitaraman,
J.A.Tainer.
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Ref.
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Embo J, 2003,
22,
4566-4576.
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PubMed id
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Abstract
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To clarify RAD51 interactions controlling homologous recombination, we report
here the crystal structure of the full-length RAD51 homolog from Pyrococcus
furiosus. The structure reveals how RAD51 proteins assemble into inactive
heptameric rings and active DNA-bound filaments matching three-dimensional
electron microscopy reconstructions. A polymerization motif (RAD51-PM) tethers
individual subunits together to form assemblies. Subunit interactions support an
allosteric 'switch' promoting ATPase activity and DNA binding roles for the
N-terminal domain helix-hairpin-helix (HhH) motif. Structural and mutational
results characterize RAD51 interactions with the breast cancer susceptibility
protein BRCA2 in higher eukaryotes. A designed P.furiosus RAD51 mutant binds BRC
repeats and forms BRCA2-dependent nuclear foci in human cells in response to
gamma-irradiation-induced DNA damage, similar to human RAD51. These results show
that BRCA2 repeats mimic the RAD51-PM and imply analogous RAD51 interactions
with RAD52 and RAD54. Both BRCA2 and RAD54 may act as antagonists and chaperones
for RAD51 filament assembly by coupling RAD51 interface exchanges with DNA
binding. Together, these structural and mutational results support an interface
exchange hypothesis for coordinated protein interactions in homologous
recombination.
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