6HD0

Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1

6HD0 の概要

• エントリーDOI: 10.2210/pdb6hd0/pdb
• 分子名称: Transitional endoplasmic reticulum ATPase, Plant UBX domain-containing protein 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: atpase, pux1, ubx, p97, disassembly, gene regulation
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 494895.20

構造登録者

Heinemann, U.,Roske, Y.,Banchenko, S. (登録日: 2018-08-17, 公開日: 2019-08-28, 最終更新日: 2024-01-17)

主引用文献

Banchenko, S.,Arumughan, A.,Petrovic, S.,Schwefel, D.,Wanker, E.E.,Roske, Y.,Heinemann, U.
Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.
Structure, 27:1830-, 2019

PubMed Abstract: The hexameric ring structure of the type II AAA+ ATPases is considered as stable and permanent. Recently, the UBX domain-containing cofactors Arabidopsis thaliana PUX1 and human alveolar soft part sarcoma locus (ASPL) were reported to bind and disassemble the cognate AAA+ ATPases AtCDC48 and human p97. Here, we present two crystal structures related to these complexes: a truncated AtCDC48 (AtCDC48-ND1) and a hybrid complex containing human p97-ND1 and the UBX domain of plant PUX1 (p97-ND1:PUX1-UBX). These structures reveal close similarity between the human and plant AAA+ ATPases, but also highlight differences between disassembling and non-disassembling AAA+ ATPase cofactors. Based on an AtCDC48 disassembly assay with PUX1 and known crystal structures of the p97-bound human cofactor ASPL, we propose a general ATPase disassembly model. Thus, our structural and biophysical investigations provide detailed insight into the mechanism of AAA+ ATPase disassembly by UBX domain cofactors and suggest a general mode of regulating the cellular activity of these molecular machines.

PubMed: 31648844
DOI: 10.1016/j.str.2019.10.001

実験手法

X-RAY DIFFRACTION (3.728 Å)