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Journal of Virology, May 2006, p. 4304-4312, Vol. 80, No. 9
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.9.4304-4312.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain{dagger}

Gretchen Meinke, Peter A. Bullock, and Andrew Bohm*

Tufts University School of Medicine and the Sackler School of Graduate Biomedical Sciences, Department of Biochemistry, 136 Harrison Avenue, Boston, Massachusetts 02111

Received 16 December 2005/ Accepted 7 February 2006

The origins of replication of DNA tumor viruses have a highly conserved feature, namely, multiple binding sites for their respective initiator proteins arranged as inverted repeats. In the 1.45-Å crystal structure of the simian virus 40 large T-antigen (T-ag) origin-binding domain (obd) reported herein, T-ag obd monomers form a left-handed spiral with an inner channel of 30 Å having six monomers per turn. The inner surface of the spiral is positively charged and includes residues known to bind DNA. Residues implicated in hexamerization of full-length T-ag are located at the interface between adjacent T-ag obd monomers. These data provide a high-resolution model of the hexamer of origin-binding domains observed in electron microscopy studies and allow the obd's to be oriented relative to the hexamer of T-ag helicase domains to which they are connected.

* Corresponding author. Mailing address: Department of Biochemistry, Tufts University, 136 Harrison Avenue, Boston, MA 02111. Phone: (617) 636-2905. Fax: (617) 636-2409. E-mail: andrew.bohm{at}tufts.edu.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, May 2006, p. 4304-4312, Vol. 80, No. 9
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.9.4304-4312.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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