抄録
The AAA + ATPase p97/VCP, helped by adaptor proteins, exerts its essential role in cellular events such as endoplasmic reticulum-associated protein degradation or the reassembly of Golgi, ER and the nuclear envelope after mitosis. Here, we report the three-dimensional cryo-electron microscopy structures at ∼20 Å resolution in two nucleotide states of the endogenous hexameric p97 in complex with a recombinant p47 trimer, one of the major p97 adaptor proteins involved in membrane fusion. Depending on the nucleotide state, we observe the p47 trimer to be in two distinct arrangements on top of the p97 hexamer. By combining the EM data with NMR and other biophysical measurements, we propose a model of ATP-dependent p97(N) domain motions that lead to a rearrangement of p47 domains, which could result in the disassembly of target protein complexes.
本文言語 | 英語 |
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ページ(範囲) | 1967-1976 |
ページ数 | 10 |
ジャーナル | EMBO Journal |
巻 | 25 |
号 | 9 |
DOI | |
出版ステータス | 出版済み - 5月 3 2006 |
外部発表 | はい |
All Science Journal Classification (ASJC) codes
- 神経科学(全般)
- 分子生物学
- 生化学、遺伝学、分子生物学(全般)
- 免疫学および微生物学(全般)