The Hub1 protein from Saccharomyces cerevisiae (NESG ID: YTYst190 / PIR: S78735/ GI: 7493880) is a ubiquitin-like modifier protein (UBL) that is essential for proper cell polarization during the formation of mating projections in S. cerevisiae. Hub1 conjugation to the cell polarity factors Sph1 and Hbt1 was required for their proper subcellular localization (1). Hub1 belongs to a conserved family of eukaryotic proteins. S. cerevisiae and human Hub1 share 65% identity. The sequence identity with ubiquitin is 22%. Here we describe the solution structure of Hub1 determined by NMR spectroscopy. We compare the structure of Hub1 to ubiquitin and find that although the overall fold is almost identical, critical surface residues in ubiquitin are not conserved in Hub1. These differences probably reflect the different functions of the UBL Hub1.
Revised: October 9, 2003 |
Published: December 1, 2003
Citation
Ramelot T.A., J.R. Cort, A. Yee, A. Semsesi, A.M. Edwards, C.H. Arrowsmith, and M.A. Kennedy. 2003.Solution Structure of the Yeast Ubiquitin-Like Modifier Protein Hub1.Journal of Structural and Functional Genomics 4, no. 1:25-30. PNWD-SA-5795.