PXD020229 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Crosslinking mass spectrometry of the unconventional kinetoplastid kinetochore protein KKT4 |
Description | The kinetochore is the macromolecular protein machine that drives chromosome segregation by interacting with spindle microtubules. Unlike most other eukaryotes that have canonical kinetochore proteins, a group of evolutionarily divergent eukaryotes called kinetoplastids (such as Trypanosoma brucei that causes human African trypanosomiasis) have a unique set of kinetochore proteins. To date, the only kinetoplastid kinetochore protein that is known to bind microtubules is KKT4, which has no high-resolution structure information available. Here we used X-ray crystallography, NMR spectroscopy, and crosslinking mass spectrometry to characterise the structure and dynamics of KKT4. |
HostingRepository | PRIDE |
AnnounceDate | 2020-10-15 |
AnnouncementXML | Submission_2020-10-15_05:43:59.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Bungo Akiyoshi |
SpeciesList | scientific name: Trypanosoma brucei; NCBI TaxID: 5691; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-07-06 16:11:49 | ID requested | |
⏵ 1 | 2020-10-15 05:43:59 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Kinetoplastid, kinetochore, KKT4, Trypanosoma brucei |
Contact List
Bungo Akiyoshi |
contact affiliation | University of Oxford |
contact email | bungo.akiyoshi@bioch.ox.ac.uk |
lab head | |
Bungo Akiyoshi |
contact affiliation | University of Oxford |
contact email | bungo.akiyoshi@bioch.ox.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD020229
- Label: PRIDE project
- Name: Crosslinking mass spectrometry of the unconventional kinetoplastid kinetochore protein KKT4