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Nucleic Acids Research Advance Access published online on December 15, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn999
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© 2008 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 a replicative hexameric helicase DnaC and its complex with single-stranded DNA

Yu-Hua Lo1,2, Kuang-Lei Tsai1,2, Yuh-Ju Sun2, Wei-Ti Chen1,2,3, Cheng-Yang Huang1 and Chwan-Deng Hsiao1,*

1Institute of Molecular Biology, Academia Sinica, Taipei, 115, 2Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300 and 3Taiwan International Graduate Program, Academia Sinica, Taipei, 115, Taiwan

*To whom correspondence should be addressed. Tel: +886 2 2788 2743; Fax: +886 2 2782 6085; Email: hsiao{at}gate.sinica.edu.tw

Received September 12, 2008. Revised November 16, 2008. Accepted November 26, 2008.

DNA helicases are motor proteins that play essential roles in DNA replication, repair and recombination. In the replicative hexameric helicase, the fundamental reaction is the unwinding of duplex DNA; however, our understanding of this function remains vague due to insufficient structural information. Here, we report two crystal structures of the DnaB-family replicative helicase from Geobacillus kaustophilus HTA426 (GkDnaC) in the apo-form and bound to single-stranded DNA (ssDNA). The GkDnaC–ssDNA complex structure reveals that three symmetrical basic grooves on the interior surface of the hexamer individually encircle ssDNA. The ssDNA-binding pockets in this structure are directed toward the N-terminal domain collar of the hexameric ring, thus orienting the ssDNA toward the DnaG primase to facilitate the synthesis of short RNA primers. These findings provide insight into the mechanism of ssDNA binding and provide a working model to establish a novel mechanism for DNA translocation at the replication fork.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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