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PDBsum entry 4cdg
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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 bloom'S syndrome helicase indicates a role for the hrdc domain in conformational changes.
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Authors
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J.A.Newman,
P.Savitsky,
C.K.Allerston,
A.H.Bizard,
Ã.–.Özer,
K.Sarlós,
Y.Liu,
E.Pardon,
J.Steyaert,
I.D.Hickson,
O.Gileadi.
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Ref.
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Nucleic Acids Res, 2015,
43,
5221-5235.
[DOI no: ]
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PubMed id
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Abstract
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Bloom's syndrome helicase (BLM) is a member of the RecQ family of DNA helicases,
which play key roles in the maintenance of genome integrity in all organism
groups. We describe crystal structures of the BLM helicase domain in complex
with DNA and with an antibody fragment, as well as SAXS and domain association
studies in solution. We show an unexpected nucleotide-dependent interaction of
the core helicase domain with the conserved, poorly characterized HRDC domain.
The BLM-DNA complex shows an unusual base-flipping mechanism with unique
positioning of the DNA duplex relative to the helicase core domains. Comparison
with other crystal structures of RecQ helicases permits the definition of
structural transitions underlying ATP-driven helicase action, and the
identification of a nucleotide-regulated tunnel that may play a role in
interactions with complex DNA substrates.
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