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PROTEIN STRUCTURE REPORT

The solution structure of the oxidative stress-related protein YggX from Escherichia coli

¹ Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada
² Department of Microbiology, University of Massachusetts, Amherst, Massachusetts 01003, USA

(RECEIVED January 13, 2005; FINAL REVISION March 7, 2005; ACCEPTED March 10, 2005)

YggX is a highly conserved protein found only in eubacteria and is proposed to be involved in the bacterial response to oxidative stress. Here we report the solution structure of YggX from Escherichia coli determined by nuclear magnetic resonance spectroscopy. The structure of YggX displays a fold consisting of two N-terminal antiparallel -sheets and three -helices, which shares significant structural similarity to the crystal structure of a hypothetical protein PA5148 from Pseudomonas aeruginosa. Previous studies propose YggX as an iron binding protein that is involved in cellular iron trafficking. Our data indicate that the protein alone does not bind iron in vitro, suggesting other cofactors or different conditions may be necessary for metal binding.

Keywords: NMR spectroscopy; protein structure; YggX; E. coli; iron-mediated oxidative damage

Abbreviations: HSQC, heteronuclear single quantum coherence • NMR, nuclear magnetic resonance • NOE, nuclear Overhauser effect • RCD, residual dipolar coupling • RMSD, root mean square deviation

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051358105.

Reprint requests to: Kalle Gehring, Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, QC H3G 1Y6, Canada; e-mail: kalle.gehring{at}mcgill.ca; fax: (514) 398-7384.

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