Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 18, Issue 2, Pages 243-257Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2008.01.007
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Funding
- NIAID NIH HHS [AI146724, R01 AI046724-06A2, R01 AI046724] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI046724] Funding Source: NIH RePORTER
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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.
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