2wvq: Difference between revisions
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==STRUCTURE OF THE HET-S N-TERMINAL DOMAIN. MUTANT D23A, P33H== | ==STRUCTURE OF THE HET-S N-TERMINAL DOMAIN. MUTANT D23A, P33H== | ||
<StructureSection load='2wvq' size='340' side='right' caption='[[2wvq]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2wvq' size='340' side='right' caption='[[2wvq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2wvq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Podas Podas]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WVQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wvn|2wvn]], [[2wvo|2wvo]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wvn|2wvn]], [[2wvo|2wvo]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wvq RCSB], [http://www.ebi.ac.uk/pdbsum/2wvq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvq OCA], [http://pdbe.org/2wvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wvq RCSB], [http://www.ebi.ac.uk/pdbsum/2wvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2wvq" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Podas]] | ||
[[Category: Buhtz, C]] | [[Category: Buhtz, C]] | ||
[[Category: Choe, S]] | [[Category: Choe, S]] | ||
Revision as of 16:18, 4 August 2016
STRUCTURE OF THE HET-S N-TERMINAL DOMAIN. MUTANT D23A, P33HSTRUCTURE OF THE HET-S N-TERMINAL DOMAIN. MUTANT D23A, P33H
Structural highlights
Function[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.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHET-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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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