PXD017353

PXD017353 is an original dataset announced via ProteomeXchange.

Title	A new twist on bacterial motility – two distinct type IV pili revealed by cryoEM
Description	Many bacteria express filaments called type IV pili on their surface, which are involved in motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Type IV pili are comprised of a helical assembly of repeating pilin subunits that allow both flexibility and strength. They are therefore powerful structures that enable bacterial proliferation and genetic adaptation, potentially leading to the development of pathogenicity and antibiotic resistance. They are also targets for drug development. By electron cryo-microscopy and mass spectrometry, we show that the bacterium Thermus thermophilus produces two forms of type IV pilus, differing in structure and protein composition. We have determined the structures of both and built atomic models, which reveal a new pilin, how the subunits assemble and their glycosylation patterns. We also delineate the roles of the two filaments in promoting twitching and natural transformation.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:00:29.639.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Julian Langer
SpeciesList	scientific name: Thermus thermophilus HB27; NCBI TaxID: 262724;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos; Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2020-01-31 07:20:31	ID requested
1	2020-03-09 00:25:16	announced
2	2020-05-15 04:03:55	announced	2020-05-15: Updated publication reference for PubMed record(s): 32376942.
⏵ 3	2024-10-22 05:00:37	announced	2024-10-22: Updated project metadata.

10.1038/s41467-020-15650-w;

Neuhaus A, Selvaraj M, Salzer R, Langer JD, Kruse K, Kirchner L, Sanders K, Daum B, Averhoff B, Gold VAM, IV pili assembled by the same bacterium. Nat Commun, 11(1):2231(2020) [pubmed]

curator keyword: Biological

submitter keyword: electron cryo-tomography, flexible filaments,Type IV pili, electron cryo-microscopy, pilin

Julian Langer
contact affiliation	Julian Langer: MPI for Biophysics and Brain Research Kate Heesom (k.heesom@bristol.ac.uk): University of Bristol Proteomics Facility
contact email	julian.langer@biophys.mpg.de
lab head
Julian Langer
contact affiliation	MPIs for Biophysics and Brain Research
contact email	julian.langer@biophys.mpg.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/03/PXD017353

PRIDE project URI

• PRIDE
  1. PXD017353
     1. Label: PRIDE project
     2. Name: A new twist on bacterial motility – two distinct type IV pili revealed by cryoEM