6HD0
Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1
Summary for 6HD0
| Entry DOI | 10.2210/pdb6hd0/pdb |
| Descriptor | Transitional endoplasmic reticulum ATPase, Plant UBX domain-containing protein 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | atpase, pux1, ubx, p97, disassembly, gene regulation |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 12 |
| Total formula weight | 494895.20 |
| Authors | Heinemann, U.,Roske, Y.,Banchenko, S. (deposition date: 2018-08-17, release date: 2019-08-28, Last modification date: 2024-01-17) |
| Primary citation | 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 Cited by 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: 31648844DOI: 10.1016/j.str.2019.10.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.728 Å) |
Structure validation
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