2wvn: Difference between revisions

Latest revision as of 10:17, 9 May 2024

Structure of the HET-s N-terminal domain

Structural highlights

2wvn is a 1 chain structure with sequence from Podospora anserina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.62Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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.

References

↑ Turcq B, Deleu C, Denayrolles M, Begueret J. Two allelic genes responsible for vegetative incompatibility in the fungus Podospora anserina are not essential for cell viability. Mol Gen Genet. 1991 Aug;228(1-2):265-9. PMID:1886611
↑ Deleu C, Clave C, Begueret J. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics. 1993 Sep;135(1):45-52. PMID:8224826
↑ Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9773-8. PMID:9275200
↑ Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R. The mechanism of prion inhibition by HET-S. Mol Cell. 2010 Jun 25;38(6):889-99. PMID:20620958 doi:10.1016/j.molcel.2010.05.019

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Turcq B, Deleu C, Denayrolles M, Begueret J. Two allelic genes responsible for vegetative incompatibility in the fungus Podospora anserina are not essential for cell viability. Mol Gen Genet. 1991 Aug;228(1-2):265-9. PMID:1886611

[2] Deleu C, Clave C, Begueret J. A single amino acid difference is sufficient to elicit vegetative incompatibility in the fungus Podospora anserina. Genetics. 1993 Sep;135(1):45-52. PMID:8224826

[3] Coustou V, Deleu C, Saupe S, Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9773-8. PMID:9275200

[4] Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R. The mechanism of prion inhibition by HET-S. Mol Cell. 2010 Jun 25;38(6):889-99. PMID:20620958 doi:10.1016/j.molcel.2010.05.019

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[4]

@@ Line 3: / Line 3: @@
 <StructureSection load='2wvn' size='340' side='right'caption='[[2wvn]], [[Resolution|resolution]] 2.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Podas Podas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2wvn]] is a 1 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=2WVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WVN FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wvo|2wvo]], [[2wvq|2wvq]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.62&#8491;</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=2wvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wvn OCA], [https://pdbe.org/2wvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wvn RCSB], [https://www.ebi.ac.uk/pdbsum/2wvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wvn 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>
+[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]]
@@ Line 36: / Line 36: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Podas]]
+[[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 regulatory domain]]
-[[Category: Prion-binding protein]]

2wvn: Difference between revisions

Latest revision as of 10:17, 9 May 2024

Structure of the HET-s N-terminal domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

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