1HQO

CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P

Summary for 1HQO

• Entry DOI: 10.2210/pdb1hqo/pdb
• Descriptor: URE2 PROTEIN (2 entities in total)
• Functional Keywords: glutathione s-transferase superfamily fold, signaling protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P23202
• Total number of polymer chains: 2
• Total formula weight: 59875.89

Authors

Umland, T.C.,Taylor, K.L.,Rhee, S.,Wickner, R.B.,Davies, D.R. (deposition date: 2000-12-18, release date: 2001-02-14, Last modification date: 2024-11-20)

Primary citation

Umland, T.C.,Taylor, K.L.,Rhee, S.,Wickner, R.B.,Davies, D.R.
The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p.
Proc.Natl.Acad.Sci.USA, 98:1459-1464, 2001

PubMed Abstract: 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.

PubMed: 11171973
DOI: 10.1073/pnas.041607898

Experimental method

X-RAY DIFFRACTION (2.3 Å)