2wvo

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Structure of the HET-S N-terminal domain

Structural highlights

2wvo is a 2 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 2.3Å
Ligands:CL
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HETS_PODAN 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). Interaction with the prion form [het-s] of incompatible cells triggers a lethal reaction that prevents the formation of viable heterokaryons.[1] [2] [3] [4]

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[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Balguerie A, Dos Reis S, Coulary-Salin B, Chaignepain S, Sabourin M, Schmitter JM, Saupe SJ. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo. J Cell Sci. 2004 May 15;117(Pt 12):2599-610. PMID:15159455 doi:http://dx.doi.org/10.1242/jcs.01116
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

Contents


PDB ID 2wvo

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