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Conformational changes in the AAA ATPase p97–p47 adaptor complex
Author(s) -
Beuron Fabienne,
Dreveny Ingrid,
Yuan Xuemei,
Pye Valerie E,
Mckeown Ciaran,
Briggs Louise C,
Cliff Matthew J,
Kaneko Yayoi,
Wallis Russell,
Isaacson Rivka L,
Ladbury John E,
Matthews Steve J,
Kondo Hisao,
Zhang Xiaodong,
Freemont Paul S
Publication year - 2006
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7601055
Subject(s) - biology , signal transducing adaptor protein , atpase , aaa proteins , protein structure , microbiology and biotechnology , computational biology , biophysics , biochemistry , signal transduction , enzyme
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.