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• W2043249713 endingPage "257" @default.
• W2043249713 startingPage "243" @default.
• W2043249713 abstract "Helicases are molecular machines that utilize energy derived from ATP hydrolysis to move along nucleic acids and to separate base-paired nucleotides. The movement of the helicase can also be described as a stationary helicase that pumps nucleic acid. Recent structural data for the hexameric E1 helicase of papillomavirus in complex with single-stranded DNA and MgADP has provided a detailed atomic and mechanistic picture of its ATP-driven DNA translocation. The structural and mechanistic features of this helicase are compared with the hexameric helicase prototypes T7gp4 and SV40 T-antigen. The ATP-binding site architectures of these proteins are structurally similar to the sites of other prototypical ATP-driven motors such as F1-ATPase, suggesting related roles for the individual site residues in the ATPase activity." @default.
• W2043249713 created "2016-06-24" @default.
• W2043249713 creator A5036421734 @default.
• W2043249713 creator A5076746607 @default.
• W2043249713 date "2008-04-01" @default.
• W2043249713 modified "2023-09-26" @default.
• W2043249713 title "On helicases and other motor proteins" @default.
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