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• W2157133034 endingPage "4297" @default.
• W2157133034 startingPage "4292" @default.
• W2157133034 abstract "Significance RecQ DNA helicases catalyze critical genome maintenance reactions in nearly all organisms. This study describes the crystal structure of a bacterial RecQ helicase bound in a productive complex with DNA. Together with biochemical experiments, the structure reveals a conserved coupling mechanism that links DNA binding to ATP hydrolysis in RecQ enzymes. These findings also help explain how structural dynamics could facilitate RecQ’s noted ability to process diverse DNA substrates. A model explaining the physical basis for RecQ substrate binding and unwinding is proposed." @default.
• W2157133034 created "2016-06-24" @default.
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• W2157133034 date "2015-03-23" @default.
• W2157133034 modified "2023-10-11" @default.
• W2157133034 title "Structural mechanisms of DNA binding and unwinding in bacterial RecQ helicases" @default.
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• W2157133034 doi "https://doi.org/10.1073/pnas.1416746112" @default.
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• W2157133034 hasPublicationYear "2015" @default.
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