Enemark, E. J., Joshua-Tor, L. (April 2008) On helicases and other motor proteins. Curr Opin Struct Biol, 18 (2). 243-257 .
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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.
| Item Type: | Paper |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > analysis and processing > molecular interaction processing bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes organism description > virus |
| CSHL Authors: | |
| Communities: | CSHL labs > Joshua-Tor lab |
| Depositing User: | Tom Adams |
| Date: | April 2008 |
| Date Deposited: | 26 Jul 2011 20:24 |
| Last Modified: | 13 Jan 2017 20:42 |
| PMCID: | PMC2396192 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/7726 |
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