1hqo
From Proteopedia
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|PDB= 1hqo |SIZE=350|CAPTION= <scene name='initialview01'>1hqo</scene>, resolution 2.3Å | |PDB= 1hqo |SIZE=350|CAPTION= <scene name='initialview01'>1hqo</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= URE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= URE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqo OCA], [http://www.ebi.ac.uk/pdbsum/1hqo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hqo RCSB]</span> | ||
}} | }} | ||
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[[Category: glutathione s-transferase superfamily fold]] | [[Category: glutathione s-transferase superfamily fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:14 2008'' |
Revision as of 18:09, 30 March 2008
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| , resolution 2.3Å | |||||||
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| Ligands: | |||||||
| Gene: | URE2 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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