Solution structure of the origin DNA-binding domain of SV40 T-antigen

Xuelian Luo, David G. Sanford, Peter A. Bullock, William W. Bachovchin

Research output: Contribution to journalArticle

95 Scopus citations

Abstract

The structure of the domain from simian virus 40 (SV40) large T-antigen that binds to the SV40 origin of DNA replication (T-ag-OBD131-260) has been determined by nuclear magnetic resonance spectroscopy. The overall fold, consisting of a central five-stranded antiparallel β-sheet flanked by two α-helices on one side and one α-helix and one 310-helix on the other, is a new one. Previous mutational analyses have identified two elements, termed A (-152-155) and B2 (203-207), as essential for origin-specific recognition. These elements form two closely juxtaposed loops that define a continuous surface on the protein. The addition of a duplex oligonucleotide containing the origin recognition pentanucleotide GAGGC induces chemical shift changes and slows amide proton exchange in resonances from this region, indicating that this surface directly contacts the DNA.

Original languageEnglish (US)
Pages (from-to)1034-1039
Number of pages6
JournalNature Structural Biology
Volume3
Issue number12
DOIs
StatePublished - Dec 1 1996

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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