NR ALVX
AU Umland,T.C.; Taylor,K.L.; Rhee,S.; Wickner,R.B.; Davies,D.R.
TI The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
QU Proceedings of the National Academy of Sciences of the United States of America 2001 Feb 13; 98(4): 1459-64
PT journal article
AB The yeast nonchromosomal gene [URE3] is due to a prion form of the nitrogen regulatory protein Ure2p. It is a negative regulator of nitrogen catabolism and acts by inhibiting the transcription factor Gln3p. Ure2p residues 1-80 are necessary for prion generation and propagation. The C-terminal fragment retains nitrogen regulatory activity, albeit somewhat less efficiently than the full-length protein, and it also lowers the frequency of prion generation. The crystal structure of this C-terminal fragment, Ure2p(97-354), at 2.3 A resolution is described here. It adopts the same fold as the glutathione S-transferase superfamily, consistent with their sequence similarity. However, Ure2p(97-354) lacks a properly positioned catalytic residue that is required for S-transferase activity. Residues within this regulatory fragment that have been indicated by mutational studies to influence prion generation have been mapped onto the three-dimensional structure, and possible implications for prion activity are discussed.
MH Amino Acid Sequence; Crystallography, X-Ray; Fungal Proteins/*chemistry/genetics; Glutathione Transferase/chemistry; Models, Molecular; Molecular Sequence Data; Nitrogen/*metabolism; Prions; Protein Structure, Secondary; Recombinant Fusion Proteins/chemistry/genetics
AD Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0560, USA
SP englisch
PO USA