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TitleStructural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex.
Journal, issue, pagesScience, Vol. 368, Issue 6489, Year 2020
Publish dateApr 24, 2020
AuthorsXudong Wu / Marc Siggel / Sergey Ovchinnikov / Wei Mi / Vladimir Svetlov / Evgeny Nudler / Maofu Liao / Gerhard Hummer / Tom A Rapoport /
PubMed AbstractMisfolded luminal endoplasmic reticulum (ER) proteins undergo ER-associated degradation (ERAD-L): They are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome. ERAD- ...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.
External linksScience / PubMed:32327568 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 4.3 Å
Structure data

21220

6vjy

EMDB-21220: Cryo-EM map of Hrd1/Hrd3 monomer
PDB-6vjy: Cryo-EM structure of Hrd1/Hrd3 monomer
Method: EM (single particle) / Resolution: 4.3 Å

21221

6vjz

EMDB-21221: CryoEM map of Hrd1-Usa1/Der1/Hrd3 complex of the expected topology
PDB-6vjz: CryoEM structure of Hrd1-Usa1/Der1/Hrd3 complex of the expected topology
Method: EM (single particle) / Resolution: 4.3 Å

21222

6vk0

EMDB-21222: CryoEM map of Hrd1-Usa1/Der1/Hrd3 of the flipped topology
PDB-6vk0: CryoEM structure of Hrd1-Usa1/Der1/Hrd3 of the flipped topology
Method: EM (single particle) / Resolution: 4.1 Å

21223

6vk1

EMDB-21223: CryoEM map of Hrd1/Hrd3 part from Hrd1-Usa1/Der1/Hrd3 complex
PDB-6vk1: CryoEM structure of Hrd1/Hrd3 part from Hrd1-Usa1/Der1/Hrd3 complex
Method: EM (single particle) / Resolution: 3.9 Å

21224

6vk3

EMDB-21224: CryoEM map of Hrd3/Yos9 complex
PDB-6vk3: CryoEM structure of Hrd3/Yos9 complex
Method: EM (single particle) / Resolution: 3.7 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN TRANSPORT / retro-translocon / ERAD / protein degradation / retro-translocation / ubiquitination / glycan recognition

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