2wvq

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(New page: '''Unreleased structure''' The entry 2wvq is ON HOLD Authors: Greenwald, J., Buhtz, C., Ritter, C., Kwiatkowski, W., Choe, S., Saupe, S., Riek, R. Description: Structure of the HET-s N...)
Current revision (10:17, 20 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2wvq is ON HOLD
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==Structure of the HET-s N-terminal domain. Mutant D23A, P33H==
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<StructureSection load='2wvq' size='340' side='right'caption='[[2wvq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wvq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Greenwald, J., Buhtz, C., Ritter, C., Kwiatkowski, W., Choe, S., Saupe, S., Riek, R.
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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>
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Description: Structure of the HET-s N-terminal domain. Mutant D23A, P33H
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2wvq" style="background-color:#fffaf0;"></div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 28 12:45:39 2009''
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==See Also==
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*[[Prion 3D structures|Prion 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Podospora anserina]]
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[[Category: Buhtz C]]
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[[Category: Choe S]]
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[[Category: Greenwald J]]
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[[Category: Kwiatkowski W]]
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[[Category: Riek R]]
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[[Category: Ritter C]]
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[[Category: Saupe SJ]]

Current revision

Structure of the HET-s N-terminal domain. Mutant D23A, P33H

PDB ID 2wvq

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