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PDBsum entry 3av0
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Recombination
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PDB id
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3av0
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the mre11-Rad50-Atpγs complex: understanding the interplay between mre11 and rad50.
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Authors
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H.S.Lim,
J.S.Kim,
Y.B.Park,
G.H.Gwon,
Y.Cho.
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Ref.
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Genes Dev, 2011,
25,
1091-1104.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Abstract
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Communication between Mre11 and Rad50 in the MR complex is critical for the
sensing, damage signaling, and repair of DNA double-strand breaks. To understand
the basis for interregulation between Mre11 and Rad50, we determined the crystal
structure of the Mre11-Rad50-ATPγS complex. Mre11 brings the two Rad50
molecules into close proximity and promotes ATPase activity by (1) holding the
coiled-coil arm of Rad50 through its C-terminal domain, (2) stabilizing the
signature motif and P loop of Rad50 via its capping domain, and (3) forming a
dimer through the nuclease domain. ATP-bound Rad50 negatively regulates the
nuclease activity of Mre11 by blocking the active site of Mre11. Hydrolysis of
ATP disengages Rad50 molecules, and, concomitantly, the flexible linker that
connects the C-terminal domain and the capping domain of Mre11 undergoes
substantial conformational change to relocate Rad50 and unmask the active site
of Mre11. Our structural and biochemical data provide insights into
understanding the interplay between Mre11 and Rad50 to facilitate efficient DNA
damage repair.
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