On helicases and other motor proteins

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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URL: https://www.ncbi.nlm.nih.gov/pubmed/18329872
DOI: 10.1016/j.sbi.2008.01.007

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: http://repository.cshl.edu/id/eprint/7726

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