Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes
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Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. / Newman, Joseph A; Savitsky, Pavel; Allerston, Charles K; Bizard, Anna H; Özer, Özgün; Sarlós, Kata; Liu, Ying; Pardon, Els; Steyaert, Jan; Hickson, Ian D; Gileadi, Opher.
In: Nucleic Acids Research, Vol. 43, No. 10, 2015, p. 5221-35.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes
AU - Newman, Joseph A
AU - Savitsky, Pavel
AU - Allerston, Charles K
AU - Bizard, Anna H
AU - Özer, Özgün
AU - Sarlós, Kata
AU - Liu, Ying
AU - Pardon, Els
AU - Steyaert, Jan
AU - Hickson, Ian D
AU - Gileadi, Opher
N1 - © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2015
Y1 - 2015
N2 - 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.
AB - 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.
U2 - 10.1093/nar/gkv373
DO - 10.1093/nar/gkv373
M3 - Journal article
C2 - 25901030
VL - 43
SP - 5221
EP - 5235
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
IS - 10
ER -
ID: 138761879