| A novel member of the split {beta}{alpha}{beta} fold: Solution structure of the hypothetical protein YML108W from Saccharomyces cerevisiae | |
Abstract/OtherAbstract
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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 <it>Saccharomyces cerevisiae</it>. 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 &bgr;-sheet with strand order 2143 and two &agr;-helices, with an overall topology of &bgr;&bgr;&agr;&bgr;&bgr;&agr;. Strand &bgr;1 runs parallel to &bgr;4, and &bgr;2:&bgr;1 and &bgr;4:&bgr;3 pairs are arranged in an antiparallel fashion. Although this fold belongs to the split &bgr;&agr;&bgr; family, it appears to be unique among this family; it is a novel arrangement of secondary structure, thereby expanding the universe of protein folds. |
Authors
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Pineda-Lucena, Antonio, Liao, Jack C.C., Cort, John R., Yee, Adelinda, Kennedy, Michael A., Edwards, Aled. M., Arrowsmith, Cheryl H. |
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Publication Detail
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Publisher : Cold Spring Harbor Laboratory Press Type : TEXT Format : text/html |
Date Detail
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2003-05-01 00:00:00.0 |
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FOR THE RECORD |
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Copyright Information
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Copyright (C) 2003, Cold Spring Harbor Laboratory Press |
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Languages : en |
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