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PROTEIN STRUCTURE REPORT

The solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: A structural homolog of the FF domain

¹ Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada
² Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada
³ Center for Advanced Biotechnology and Medicine (CABM), Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA
⁴ Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99354, USA
⁵ Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, USA
⁶ Washington State University, Tri-Cities, Richland, Washington 99354, USA
⁷ Department of Biochemistry and Protein Network Research Center, College of Science, Yonsei University, Seoul, Korea

(RECEIVED September 28, 2007; FINAL REVISION November 19, 2007; ACCEPTED November 20, 2007)

The ribosomal protein S17E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. S17E is a 62-residue protein conserved in archaea and eukaryotes and has no counterparts in bacteria. Mammalian S17E is a phosphoprotein component of eukaryotic ribosomes. Archaeal S17E proteins range from 59 to 79 amino acids, and are about half the length of the eukaryotic homologs which have an additional C-terminal region. Here we report the three-dimensional solution structure of S17E. S17E folds into a small three-helix bundle strikingly similar to the FF domain of human HYPA/FBP11, a novel phosphopeptide-binding fold. S17E bears a conserved positively charged surface acting as a robust scaffold for molecular recognition. The structure of M. thermoautotrophicum S17E provides a template for homology modeling of eukaryotic S17E proteins in the family.

Keywords: heteronuclear NMR; Methanobacterium thermoautotrophicum ; ribosomal protein S17E; Northeast Structural Genomics Consortium

Reprint requests to: Cheryl H. Arrowsmith, Room 4-803, TMDT, MaRS, 101 College Street, Toronto, ON M5G 1L7, Canada; e-mail: carrow{at}uhnres.utoronto.ca; fax: +1(416) 946-0881.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.073272208.

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