2WVO

Structure of the HET-S N-terminal domain

2WVO の概要

• エントリーDOI: 10.2210/pdb2wvo/pdb
• 関連するPDBエントリー: 2WVN 2WVQ
• 分子名称: SMALL S PROTEIN, CHLORIDE ION (3 entities in total)
• 機能のキーワード: prion-binding protein, prion regulatory domain, heterokaryon incompatibility
• 由来する生物種: PODOSPORA ANSERINA
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52455.31

構造登録者

Greenwald, J.,Buhtz, C.,Ritter, C.,Kwiatkowski, W.,Choe, S.,Saupe, S.J.,Riek, R. (登録日: 2009-10-19, 公開日: 2010-07-28, 最終更新日: 2023-12-20)

主引用文献

Greenwald, J.,Buhtz, C.,Ritter, C.,Kwiatkowski, W.,Choe, S.,Maddelein, M.L.,Ness, F.,Cescau, S.,Soragni, A.,Leitz, D.,Saupe, S.J.,Riek, R.
The Mechanism of Prion Inhibition by Het-S.
Mol.Cell, 38:889-, 2010

PubMed Abstract: 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.

PubMed: 20620958
DOI: 10.1016/J.MOLCEL.2010.05.019

実験手法

X-RAY DIFFRACTION (2.3 Å)