Structure of the replicative helicase of the oncoprotein SV40 large tumour antigen

Dawei Li, Rui Zhao, Wayne Lilyestrom, Dahai Gai, Rongguang Zhang, James A. DeCaprio, Ellen Fanning, Andrzej Jochimiak, Gerda Szakonyi and Xiaojiang S. Chen ()
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Dawei Li: University of Colorado Health Science Center, School of Medicine
Rui Zhao: University of Colorado Health Science Center, School of Medicine
Wayne Lilyestrom: University of Colorado Health Science Center, School of Medicine
Dahai Gai: University of Colorado Health Science Center, School of Medicine
Rongguang Zhang: Advanced Photon Source, SBC, Argonne National Laboratory
James A. DeCaprio: Medical Oncology, Dana-Farber Cancer Institute
Ellen Fanning: Vanderbilt University
Andrzej Jochimiak: Advanced Photon Source, SBC, Argonne National Laboratory
Gerda Szakonyi: University of Colorado Health Science Center, School of Medicine
Xiaojiang S. Chen: University of Colorado Health Science Center, School of Medicine

Nature, 2003, vol. 423, issue 6939, 512-518

Abstract: Abstract The oncoprotein large tumour antigen (LTag) is encoded by the DNA tumour virus simian virus 40. LTag transforms cells and induces tumours in animals by altering the functions of tumour suppressors (including pRB and p53) and other key cellular proteins. LTag is also a molecular machine that distorts/melts the replication origin of the viral genome and unwinds duplex DNA. LTag therefore seems to be a functional homologue of the eukaryotic minichromosome maintenance (MCM) complex. Here we present the X-ray structure of a hexameric LTag with DNA helicase activity. The structure identifies the p53-binding surface and reveals the structural basis of hexamerization. The hexamer contains a long, positively charged channel with an unusually large central chamber that binds both single-stranded and double-stranded DNA. The hexamer organizes into two tiers that can potentially rotate relative to each other through connecting α-helices to expand/constrict the channel, producing an ‘iris’ effect that could be used for distorting or melting the origin and unwinding DNA at the replication fork.

Date: 2003
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DOI: 10.1038/nature01691

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