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PDBsum entry 1oyy
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Contents |
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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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High-Resolution structure of the e.Coli recq helicase catalytic core.
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Authors
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D.A.Bernstein,
M.C.Zittel,
J.L.Keck.
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Ref.
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Embo J, 2003,
22,
4910-4921.
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PubMed id
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Abstract
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RecQ family helicases catalyze critical genome maintenance reactions in
bacterial and eukaryotic cells, playing key roles in several DNA metabolic
processes. Mutations in recQ genes are linked to genome instability and human
disease. To define the physical basis of RecQ enzyme function, we have
determined a 1.8 A resolution crystal structure of the catalytic core of
Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of
the core bound to the ATP analog ATPgammaS. The RecQ core comprises four
conserved subdomains; two of these combine to form its helicase region, while
the others form unexpected Zn(2+)-binding and winged-helix motifs. The
structures reveal the molecular basis of missense mutations that cause Bloom's
syndrome, a human RecQ-associated disease. Finally, based on findings from the
structures, we propose a mechanism for RecQ activity that could explain its
functional coordination with topoisomerase III.
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