| Autor: |
Pineda-Lucena, Antonio, Liao, Jack C.C., Cort, John R., Yee, Adelinda, Kennedy, Michael A., Edwards, Aled. M., Arrowsmith, Cheryl H. |
| Zdroj: |
Protein Science: A Publication of the Protein Society; 2003, Vol. 12 Issue 5, p1136-1140, 5p |
| Abstrakt: |
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 β-sheet with strand order 2143 and two α-helices, with an overall topology of ββαββα. Strand β1 runs parallel to β4, and β2:β1 and β4:β3 pairs are arranged in an antiparallel fashion. Although this fold belongs to the split βαβ family, it appears to be unique among this family; it is a novel arrangement of secondary structure, thereby expanding the universe of protein folds. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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