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Nucleic Acids Research Advance Access originally published online on July 1, 2007
Nucleic Acids Research 2007 35(14):4728-4736; doi:10.1093/nar/gkm507
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Nucleic Acids Research, 2007, Vol. 35, No. 14 4728-4736
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

The crystal structure of the Thermus aquaticus DnaB helicase monomer

Scott Bailey1,3, William K. Eliason1,3 and Thomas A. Steitz1,2,3,*

1Department of Molecular Biophysics and Biochemistry, 2Department of Chemistry and 3Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA

*To whom correspondence should be addressed. Tel: +1 203 432 5619; Fax: +1 203 432 3282; Email: eatherton{at}csb.yale.edu

Received April 10, 2007. Revised June 5, 2007. Accepted June 11, 2007.

The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 Å resolution. DnaB is a highly flexible two domain protein. The C-terminal domain exhibits a RecA-like core fold and contains all the conserved sequence motifs that are characteristic of the DnaB helicase family. The N-terminal domain contains an additional helical hairpin that makes it larger than previously appreciated. Several DnaB mutations that modulate its interaction with primase are found in this hairpin. The similarity in the fold of the DnaB N-terminal domain with that of the C-terminal helicase-binding domain (HBD) of the DnaG primase also includes this hairpin. Comparison of hexameric homology models of DnaB with the structure of the papillomavirus E1 helicase suggests the two helicases may function through different mechanisms despite their sharing a common ancestor.


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