1hqo
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P''' | '''CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P''' | ||
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[[Category: Umland, T C.]] | [[Category: Umland, T C.]] | ||
[[Category: Wickner, R B.]] | [[Category: Wickner, R B.]] | ||
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Revision as of 16:07, 2 May 2008
CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P
Overview
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.
About this Structure
1HQO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p., Umland TC, Taylor KL, Rhee S, Wickner RB, Davies DR, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1459-64. Epub 2001 Feb 6. PMID:11171973 Page seeded by OCA on Fri May 2 19:07:58 2008
