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lüll On helicases and other motor proteins Enemark EJ; Joshua-Tor LCurr Opin Struct Biol 2008[Apr]; 18 (2): 243-57Helicases 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.|Adenosine Triphosphate/metabolism[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|DNA Helicases/*chemistry/*metabolism[MESH]|DNA/chemistry/metabolism[MESH]|Molecular Motor Proteins/*metabolism[MESH]|Molecular Sequence Data[MESH]|RNA Helicases/*chemistry/*metabolism[MESH] |