1hqo: Difference between revisions

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-[[Image:1hqo.png|left|200px]]
-{{STRUCTURE_1hqo|  PDB=1hqo  |  SCENE=  }}
+==CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P==
+<StructureSection load='1hqo' size='340' side='right'caption='[[1hqo]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1hqo]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQO FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqo OCA], [https://pdbe.org/1hqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqo RCSB], [https://www.ebi.ac.uk/pdbsum/1hqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqo ProSAT]</span></td></tr>
+</table>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hqo ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===CRYSTAL STRUCTURE OF THE NITROGEN REGULATION FRAGMENT OF THE YEAST PRION PROTEIN URE2P===
+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<ref>PMID:11171973</ref>
-{{ABSTRACT_PUBMED_11171973}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1hqo" style="background-color:#fffaf0;"></div>
-[[1hqo]] is a 2 chain structure of [[Prion]] with 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].
 ==See Also==
-*[[Prion|Prion]]
+*[[Prion 3D structures|Prion 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011171973</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Davies, D R.]]
+[[Category: Davies DR]]
-[[Category: Rhee, S.]]
+[[Category: Rhee S]]
-[[Category: Taylor, K L.]]
+[[Category: Taylor KL]]
-[[Category: Umland, T C.]]
+[[Category: Umland TC]]
-[[Category: Wickner, R B.]]
+[[Category: Wickner RB]]
-[[Category: Glutathione s-transferase superfamily fold]]
-[[Category: Signaling protein]]