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-Structure paper
タイトル | Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 109, Issue 4, Page 1098-1103, Year 2012 |
掲載日 | 2012年1月24日 |
著者 | Cecilia Bebeacua / Andreas Förster / Ciarán McKeown / Hemmo H Meyer / Xiaodong Zhang / Paul S Freemont / |
PubMed 要旨 | p97 is a key regulator of numerous cellular pathways and associates with ubiquitin-binding adaptors to remodel ubiquitin-modified substrate proteins. How adaptor binding to p97 is coordinated and how ...p97 is a key regulator of numerous cellular pathways and associates with ubiquitin-binding adaptors to remodel ubiquitin-modified substrate proteins. How adaptor binding to p97 is coordinated and how adaptors contribute to substrate remodeling is unclear. Here we present the 3D electron cryomicroscopy reconstructions of the major Ufd1-Npl4 adaptor in complex with p97. Our reconstructions show that p97-Ufd1-Npl4 is highly dynamic and that Ufd1-Npl4 assumes distinct positions relative to the p97 ring upon addition of nucleotide. Our results suggest a model for substrate remodeling by p97 and also explains how p97-Ufd1-Npl4 could form other complexes in a hierarchical model of p97-cofactor assembly. |
リンク | Proc Natl Acad Sci U S A / PubMed:22232657 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 23.0 - 28.0 Å |
構造データ | EMDB-2013: EMDB-2014: EMDB-2015: EMDB-2016: |
由来 |
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