6VJY
Cryo-EM structure of Hrd1/Hrd3 monomer
6VJY の概要
エントリーDOI | 10.2210/pdb6vjy/pdb |
EMDBエントリー | 21220 |
分子名称 | ERAD-associated E3 ubiquitin-protein ligase HRD1, ERAD-associated E3 ubiquitin-protein ligase component HRD3 (2 entities in total) |
機能のキーワード | retro-translocon, erad, protein degradation, protein transport |
由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 138504.98 |
構造登録者 | |
主引用文献 | Wu, X.,Siggel, M.,Ovchinnikov, S.,Mi, W.,Svetlov, V.,Nudler, E.,Liao, M.,Hummer, G.,Rapoport, T.A. Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex. Science, 368:-, 2020 Cited by PubMed Abstract: Misfolded luminal endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. ERAD-L is mediated by the Hrd1 complex (composed of Hrd1, Hrd3, Der1, Usa1, and Yos9), but the mechanism of retrotranslocation remains mysterious. Here, we report a structure of the active Hrd1 complex, as determined by cryo-electron microscopy analysis of two subcomplexes. Hrd3 and Yos9 jointly create a luminal binding site that recognizes glycosylated substrates. Hrd1 and the rhomboid-like Der1 protein form two "half-channels" with cytosolic and luminal cavities, respectively, and lateral gates facing one another in a thinned membrane region. These structures, along with crosslinking and molecular dynamics simulation results, suggest how a polypeptide loop of an ERAD-L substrate moves through the ER membrane. PubMed: 32327568DOI: 10.1126/science.aaz2449 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.3 Å) |
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