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J. Biol. Chem., Vol. 282, Issue 47, 34392-34400, November 23, 2007

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Crystallographic and NMR Analyses of UvsW and UvsW.1 from Bacteriophage T4^*

Iain D. Kerr¹², Sivashankar Sivakolundu¹³, Zhenmei Li, Jeffrey C. Buchsbaum, Luke A. Knox, Richard Kriwacki^¶4, and Stephen W. White^¶5

From the Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, the Department of Radiation Oncology, Milton S. Hershey Medical Center, Penn State University, Hershey, Pennsylvania 17033, and the ^¶Department of Molecular Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163

The uvsWXY system is implicated in the replication and repair of the bacteriophage T4 genome. Whereas the roles of the recombinase (UvsX) and the recombination mediator protein (UvsY) are known, the precise role of UvsW is unclear. Sequence analysis identifies UvsW as a member of the monomeric SF2 helicase superfamily that translocates nucleic acid substrates via the action of two RecA-like motor domains. Functional homologies to Escherichia coli RecG and biochemical analyses have shown that UvsW interacts with branched nucleic acid substrates, suggesting roles in recombination and the rescue of stalled replication forks. A sequencing error at the 3'-end of the uvsW gene has revealed a second, short open reading frame that encodes a protein of unknown function called UvsW.1. We have determined the crystal structure of UvsW to 2.7Å and the NMR solution structure of UvsW.1. UvsW has a four-domain architecture with structural homology to the eukaryotic SF2 helicase, Rad54. A model of the UvsW-ssDNA complex identifies structural elements and conserved residues that may interact with nucleic acid substrates. The NMR solution structure of UvsW.1 reveals a dynamic four-helix bundle with homology to the structure-specific nucleic acid binding module of RecQ helicases.

Received for publication, July 18, 2007 , and in revised form, September 17, 2007.

The atomic coordinates and structure factors (code 1RIF and 2JPN) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported in part by National Institutes of Health Grant GM66934 (to S. W. W.), Cancer Center Core Grant CA21765, and the American Lebanese Syrian Associated Charities (ALSAC). Use of the Advanced Photon Source was supported by the United States Dept. of Energy, Office of Science, Office of Basic Energy Sciences, under Contract No. W-31-109-Eng-38. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors made equal contributions to this work.

² Current address: Dept. of Cellular and Molecular Pharmacology, University of California, San Francisco, 1700 4th St., Byers Hall Rm. 509, San Francisco, CA 94158.

³ Current address: Bruker BioSpin Corp., 15 Fortune Dr., Billerica, MA 01821-3991.

⁴ To whom correspondence may be addressed: Dept. of Structural Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale St., Memphis, TN 38105. Tel.: 901-495-3290; E-mail: Richard.Kriwacki{at}stjude.org.

⁵ To whom correspondence may be addressed: Dept. of Structural Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale St., Memphis, TN 38105. Tel.: 901-495-3040; E-mail: Stephen.White{at}stjude.org.

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