6OPC

Cdc48 Hexamer in a complex with substrate and Shp1(Ubx Domain)

Summary for 6OPC

• Entry DOI: 10.2210/pdb6opc/pdb
• EMDB information: 20149
• Descriptor: Cell division control protein 48, Substrate bound to the central pore of the Cdc48 hexamer, UBX domain-containing protein 1, ... (6 entities in total)
• Functional Keywords: cdc48, aaa+ atpase, substrate translocation, motor protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 606567.42

Authors

Cooney, I.,Han, H.,Stewart, M.,Carson, R.H.,Hansen, D.,Price, J.C.,Hill, C.P.,Shen, P.S. (deposition date: 2019-04-24, release date: 2019-07-10, Last modification date: 2024-03-20)

Primary citation

Cooney, I.,Han, H.,Stewart, M.G.,Carson, R.H.,Hansen, D.T.,Iwasa, J.H.,Price, J.C.,Hill, C.P.,Shen, P.S.
Structure of the Cdc48 segregase in the act of unfolding an authentic substrate.
Science, 365:502-505, 2019

PubMed Abstract: The cellular machine Cdc48 functions in multiple biological pathways by segregating its protein substrates from a variety of stable environments such as organelles or multi-subunit complexes. Despite extensive studies, the mechanism of Cdc48 has remained obscure, and its reported structures are inconsistent with models of substrate translocation proposed for other AAA+ ATPases (adenosine triphosphatases). Here, we report a 3.7-angstrom-resolution structure of Cdc48 in complex with an adaptor protein and a native substrate. Cdc48 engages substrate by adopting a helical configuration of substrate-binding residues that extends through the central pore of both of the ATPase rings. These findings indicate a unified hand-over-hand mechanism of protein translocation by Cdc48 and other AAA+ ATPases.

PubMed: 31249134
DOI: 10.1126/science.aax0486

Experimental method

ELECTRON MICROSCOPY (3.7 Å)