Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.

Structure (London, England : 1993) - 3 Dec 2019

Banchenko Sofia, Arumughan Anup, Petrović Saša, Schwefel David, Wanker Erich E, Roske Yvette, Heinemann Udo

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ATPases Associated with Diverse Cellular Activities
Share to Coenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

Share to Protein Multimerization

Share to Protein Stability

Share to Structural Homology, Protein

Source

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.PMID 31648844Read ↗

Protein domain-domain interactions and requirements for the negative regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory X (UBX) domain-containing protein, PUX1.Semantic proximity Read ↗

Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers.Semantic proximity Read ↗

Structure and function of the AAA+ ATPase p97/Cdc48p.Semantic proximity Read ↗

Faf1 accelerates p97-mediated protein unfolding by promoting ubiquitin engagementSemantic proximity Read ↗

D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP.Semantic proximity Read ↗

Interaction between the AAA+ ATPase p97 and its cofactor ataxin3 in health and disease: Nucleotide-induced conformational changes regulate cofactor binding.Semantic proximity Read ↗

AAA+ superfamily ATPases: common structure--diverse function.Semantic proximity Read ↗

AAA+ ATPases: achieving diversity of function with conserved machinery.Semantic proximity Read ↗

Evolutionary relationships and structural mechanisms of AAA+ proteins.Semantic proximity Read ↗

Crystal structure of the catalytic D2 domain of the AAA+ ATPase p97 reveals a putative helical split-washer-type mechanism for substrate unfolding.Semantic proximity Read ↗

Crystal structures of the UBX domain of human UBXD7 and its complex with p97 ATPase.Semantic proximity Read ↗

ATP-bound form of the D1 AAA domain inhibits an essential function of Cdc48p/p97.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.