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TitleThe cryo-EM structure of the human ERAD retrotranslocation complex.
Journal, issue, pagesSci Adv, Vol. 9, Issue 41, Page eadi5656, Year 2023
Publish dateOct 13, 2023
AuthorsBing Rao / Qian Wang / Deqiang Yao / Ying Xia / Wenguo Li / Yuming Xie / Shaobai Li / Mi Cao / Yafeng Shen / An Qin / Jie Zhao / Yu Cao /
PubMed AbstractEndoplasmic reticulum-associated degradation (ERAD) maintains protein homeostasis by retrieving misfolded proteins from the endoplasmic reticulum (ER) lumen into the cytosol for degradation. The ...Endoplasmic reticulum-associated degradation (ERAD) maintains protein homeostasis by retrieving misfolded proteins from the endoplasmic reticulum (ER) lumen into the cytosol for degradation. The retrotranslocation of misfolded proteins across the ER membrane is an energy-consuming process, with the detailed transportation mechanism still needing clarification. We determined the cryo-EM structures of the hetero-decameric complex formed by the Derlin-1 tetramer and the p97 hexamer. It showed an intriguing asymmetric complex and a putative coordinated squeezing movement in Derlin-1 and p97 parts. With the conformational changes of p97 induced by its ATP hydrolysis activities, the Derlin-1 channel could be torn into a "U" shape with a large opening to the lipidic environment, thereby forming an entry for the substrates in the ER membrane. The EM analysis showed that p97 formed a functional protein complex with Derlin-1, revealing the coupling mechanism between the ERAD retrotranslocation and the ATP hydrolysis activities.
External linksSci Adv / PubMed:37831771 / PubMed Central
MethodsEM (single particle)
Resolution3.61 - 4.51 Å
Structure data

33608

7y4w

EMDB-33608, PDB-7y4w:
The cryo-EM structure of human ERAD retro-translocation complex
Method: EM (single particle) / Resolution: 3.67 Å

33611

7y53

EMDB-33611, PDB-7y53:
The cryo-EM structure of human ERAD retro-translocation complex
Method: EM (single particle) / Resolution: 3.61 Å

33613

7y59

EMDB-33613, PDB-7y59:
The cryo-EM structure of human ERAD retro-translocation complex
Method: EM (single particle) / Resolution: 4.51 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ERAD

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