PXD009732

PXD009732 is an original dataset announced via ProteomeXchange.

Title	Native mass spectrometry of ClpB
Description	The ATP-dependent bacterial protein disaggregation machine, ClpB belonging to the AAA+ superfamily, refolds toxic protein aggregates into the native state in cooperation with the cognate Hsp70 partner. The ring-shaped hexamers of ClpB unfold and thread its protein substrate through the central pore. However, their function-related structural dynamics has remained elusive. Here we directly visualize ClpB using high-speed atomic force microscopy (HS-AFM) to gain a mechanistic insight into its disaggregation function. The HS-AFM movies demonstrate massive conformational changes of the hexameric ring during ATP hydrolysis, from a round ring to a spiral and even to a pair of twisted half-spirals. HS-AFM observations of Walker-motif mutants unveil crucial roles of ATP binding and hydrolysis in the oligomer formation and structural dynamics. Furthermore, repressed and hyperactive mutations result in significantly different oligomeric forms. These results provide a comprehensive view for the ATP-driven oligomeric-state transitions that enable ClpB to disentangle protein aggregates
HostingRepository	PRIDE
AnnounceDate	2018-10-18
AnnouncementXML	Submission_2018-10-18_03:08:21.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Kentaro Ishii
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	No PTMs are included in the dataset
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2018-05-09 09:34:18	ID requested
⏵ 1	2018-10-18 03:08:23	announced

Uchihashi T, Watanabe YH, Nakazaki Y, Yamasaki T, Watanabe H, Maruno T, Ishii K, Uchiyama S, Song C, Murata K, Iino R, Ando T, Dynamic structural states of ClpB involved in its disaggregation function. Nat Commun, 9(1):2147(2018) [pubmed]

curator keyword: Biological

submitter keyword: Native mass spectrometry, ClpB

Susumu Uchiyama
contact affiliation	5Department of Biotechnology, Graduate School of Engineering, Osaka University
contact email	suchi@bio.eng.osaka-u.ac.jp
lab head
Kentaro Ishii
contact affiliation	Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences
contact email	ishii@ims.ac.jp
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009732
     1. Label: PRIDE project
     2. Name: Native mass spectrometry of ClpB