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Protein Science (2003), 12:1136-1140.
Copyright © 2003 The Protein Society

FOR THE RECORD

A novel member of the split ß{alpha}ß fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae

Antonio Pineda-Lucena1, Jack C.C. Liao1, John R. Cort2, Adelinda Yee1, Michael A. Kennedy2, Aled. M. Edwards1 and Cheryl H. Arrowsmith1

1 Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada
2 Biological Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, USA

Reprint requests to: Cheryl H. Arrowsmith, Ontario Cancer Institute, 610 University Avenue, Toronto, Ontario M5G 2M9, Canada; e-mail: carrow{at}uhnres.utoronto.ca; fax: (416) 946-6529.

As part of the Northeast Structural Genomics Consortium pilot project focused on small eukaryotic proteins and protein domains, we have determined the NMR structure of the protein encoded by ORF YML108W from Saccharomyces cerevisiae. YML108W belongs to one of the numerous structural proteomics targets whose biological function is unknown. Moreover, this protein does not have sequence similarity to any other protein. The NMR structure of YML108W consists of a four-stranded ß-sheet with strand order 2143 and two {alpha}-helices, with an overall topology of ßß{alpha}ßß{alpha}. Strand ß1 runs parallel to ß4, and ß2:ß1 and ß4:ß3 pairs are arranged in an antiparallel fashion. Although this fold belongs to the split ß{alpha}ß family, it appears to be unique among this family; it is a novel arrangement of secondary structure, thereby expanding the universe of protein folds.

Keywords: Heteronuclear NMR; protein fold; Saccharomyces cerevisiae; structural proteomics


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