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• W2026957636 abstract "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." @default.
• W2026957636 created "2016-06-24" @default.
• W2026957636 creator A5037642239 @default.
• W2026957636 date "2003-10-01" @default.
• W2026957636 modified "2023-09-23" @default.
• W2026957636 title "High-resolution structure of the E.coli RecQ helicase catalytic core" @default.
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• W2026957636 doi "https://doi.org/10.1093/emboj/cdg500" @default.
• W2026957636 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/204483" @default.
• W2026957636 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14517231" @default.
• W2026957636 hasPublicationYear "2003" @default.
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