1hqo: Difference between revisions

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New page: left|200px<br /><applet load="1hqo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqo, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1hqo.jpg|left|200px]]<br /><applet load="1hqo" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hqo.jpg|left|200px]]<br /><applet load="1hqo" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1hqo, resolution 2.3&Aring;" />
caption="1hqo, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P'''<br />
'''CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P'''<br />


==Overview==
==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.
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==
==About this Structure==
1HQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQO OCA].  
1HQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQO OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Davies, D.R.]]
[[Category: Davies, D R.]]
[[Category: Rhee, S.]]
[[Category: Rhee, S.]]
[[Category: Taylor, K.L.]]
[[Category: Taylor, K L.]]
[[Category: Umland, T.C.]]
[[Category: Umland, T C.]]
[[Category: Wickner, R.B.]]
[[Category: Wickner, R B.]]
[[Category: glutathione s-transferase superfamily fold]]
[[Category: glutathione s-transferase superfamily fold]]


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Revision as of 14:03, 21 February 2008

File:1hqo.jpg


1hqo, resolution 2.3Å

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

OverviewOverview

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 StructureAbout this Structure

1HQO is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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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