2wvq: Difference between revisions

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-[[Image:2wvq.png|left|200px]]
-{{STRUCTURE_2wvq|  PDB=2wvq  |  SCENE=  }}
+==Structure of the HET-s N-terminal domain. Mutant D23A, P33H==
+<StructureSection load='2wvq' size='340' side='right'caption='[[2wvq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2wvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVQ 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&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=DTU:(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL'>DTU</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=2wvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvq OCA], [https://pdbe.org/2wvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvq RCSB], [https://www.ebi.ac.uk/pdbsum/2wvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HETS_PODAS HETS_PODAS] Responsible for heterokaryon incompatibility, a process that ensures that during spontaneous, vegetative cell fusion only compatible cells from the same colony survive (non-self-recognition). Forms a prion for the non-Mendelian trait [het-s]. Interacts with het-S from incompatible cells to trigger a lethal reaction that prevents the formation of viable heterokaryons. It is unknown if the native, soluble protein has a cellular function.<ref>PMID:1886611</ref> <ref>PMID:8224826</ref> <ref>PMID:9275200</ref>
+== 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/wv/2wvq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2wvq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+HET-S (97% identical to HET-s) has an N-terminal globular domain that exerts a prion-inhibitory effect in cis on its own prion-forming domain (PFD) and in trans on HET-s prion propagation. We show that HET-S fails to form fibrils in vitro and that it inhibits HET-s PFD fibrillization in trans. In vivo analyses indicate that beta-structuring of the HET-S PFD is required for HET-S activity. The crystal structures of the globular domains of HET-s and HET-S are highly similar, comprising a helical fold, while NMR-based characterizations revealed no differences in the conformations of the PFDs. We conclude that prion inhibition is not encoded by structure but rather in stability and oligomerization properties: when HET-S forms a prion seed or is incorporated into a HET-s fibril via its PFD, the beta-structuring in this domain induces a change in its globular domain, generating a molecular species that is incompetent for fibril growth.
-===STRUCTURE OF THE HET-S N-TERMINAL DOMAIN. MUTANT D23A, P33H===
+The mechanism of prion inhibition by HET-S.,Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R Mol Cell. 2010 Jun 25;38(6):889-99. PMID:20620958<ref>PMID:20620958</ref>
-{{ABSTRACT_PUBMED_20620958}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2wvq" style="background-color:#fffaf0;"></div>
-[[2wvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Podospora_anserina Podospora anserina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVQ OCA].
 ==See Also==
-*[[Prion|Prion]]
+*[[Prion 3D structures|Prion 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:020620958</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Podospora anserina]]
-[[Category: Buhtz, C.]]
+[[Category: Buhtz C]]
-[[Category: Choe, S.]]
+[[Category: Choe S]]
-[[Category: Greenwald, J.]]
+[[Category: Greenwald J]]
-[[Category: Kwiatkowski, W.]]
+[[Category: Kwiatkowski W]]
-[[Category: Riek, R.]]
+[[Category: Riek R]]
-[[Category: Ritter, C.]]
+[[Category: Ritter C]]
-[[Category: Saupe, S J.]]
+[[Category: Saupe SJ]]
-[[Category: Heterokaryon incompatibility]]
-[[Category: Prion]]
-[[Category: Prion regulatory domain]]
-[[Category: Prion- binding protein]]
-[[Category: Prion-binding protein]]