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PXD033451-2

PXD033451 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleHuman P47 interactome for comparison against CryoEM data
Descriptionp97 is an essential and abundant AAA+ ATPase that unfolds ubiquitylated substrates and is a central regulator of protein homeostasis. Here we report two cryo-EM structures of human p97 in complex with its p47 adaptor. One of the conformations is six-fold symmetric, corresponds to previously reported structures of p97, and lacks bound substrate. The other structure adopts a helical conformation, displays substrate running in an extended conformation through the pore of the p97 hexamer, and resembles structures reported for other AAA unfoldases. These findings support the model that p97 utilizes a “hand-over-hand” mechanism in which two residues of the substrate are translocated for hydrolysis of two ATPs, one in each of the two p97 AAA ATPase rings. Proteomics analysis supports the model that one p97 complex can bind multiple substrate adaptors or binding partners, and can process substrates with multiple types of ubiquitin modification
HostingRepositoryPRIDE
AnnounceDate2022-05-16
AnnouncementXMLSubmission_2022-05-16_05:58:10.150.xml
DigitalObjectIdentifierhttps://dx.doi.org/10.6019/PXD033451
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterJohn Price
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListiodoacetamide derivatized residue
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02022-04-25 04:27:18ID requested
12022-05-16 05:50:58announced
22022-05-16 05:58:10announced2022-05-16: Updated publication reference for PubMed record(s): 35552390.
Publication List
Xu Y, Han H, Cooney I, Guo Y, Moran NG, Zuniga NR, Price JC, Hill CP, Shen PS, Active conformation of the p97-p47 unfoldase complex. Nat Commun, 13(1):2640(2022) [pubmed]
Keyword List
submitter keyword: Flag, affinity purification, HEK293
Contact List
John C. Price
contact affiliationBrigham Young University
contact emaildrjohncprice@gmail.com
lab head
John Price
contact affiliationBrigham Young University
contact emaildrjohncprice@gmail.com
dataset submitter
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Dataset FTP location
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PRIDE project URI
Repository Record List
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