Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy

被引：38
作者：
Bebeacua, Cecilia [1 ,2 ]
Foerster, Andreas [1 ,2 ]
McKeown, Ciaran [1 ,2 ]
Meyer, Hemmo H. [3 ]
Zhang, Xiaodong [1 ,2 ]
Freemont, Paul S. [1 ,2 ]
机构：
[1] Univ London Imperial Coll Sci Technol & Med, Struct Biol Ctr, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, Ctr Biomol Elect Microscopy, Div Mol Biosci, London SW7 2AZ, England
[3] Univ Duisburg Essen, Mol Biol Lab, Fac Biol, Ctr Med Biotechnol, D-45117 Essen, Germany
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2012年 / 109卷 / 04期
基金：
英国惠康基金;
关键词：
ATPase; electron microscopy; mechanism; structure; asymmetric complex; AAA-ATPASE P97; 3-DIMENSIONAL RECONSTRUCTION; TRANSCRIPTION FACTOR; STRUCTURAL INSIGHTS; AURORA-B; UBIQUITIN; BINDING; P97/VCP; CYCLE; CDC48/P97;
D O I：
10.1073/pnas.1114341109
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
引用
收藏
页码：1098 / 1103
页数：6
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