PXD035847 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Thriving in the heat – Lysine acetylation stabilizes the quaternary structure of a Mega-Dalton hyperthermoactive PEP-synthase |
Description | Over time structural adaptations enabled proteins and enzymes to have sufficient stability and flexibility to perform the basic functions of life under various environmental conditions. The catalytic cores of key metabolic enzymes of hyperthermophilic archaea work at a temperature range of 80-120 °C, similar to the conditions wher the earliest life forms may have thrived. Here we characterize a key enzyme of the central carbon metabolism of Pyrococcus furious, through an integrative approach combining structural mass spectrometry, cryo-electron microscopy, mass photometry and molecular modelling with molecular dynamics simulations. From our investigation, we unveil the structural organization of phosphoenolpyruvate synthase (PPSA). Its 24-meric assembly - weighing over 2 MDa - harbors flexible distal domains, whose proper functioning and coordination depends on widespread chemical acetylation of lysine residues. This non-enzymatic post-translational modification, along with other types of lysine modifications, also occurs on most other major protein complexes of P. furiosus. These modifications likely originated in the chemically favorable primordial conditions and gradually became highly specialized and enzyme-driven in more distantly related mesophiles and Eukaryotes. |
HostingRepository | PRIDE |
AnnounceDate | 2022-08-08 |
AnnouncementXML | Submission_2022-08-08_07:23:07.470.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Pascal Albanese |
SpeciesList | scientific name: Pyrococcus furiosus DSM 3638; NCBI TaxID: 186497; |
ModificationList | phosphorylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF; Orbitrap Exploris 480; Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-08-07 03:06:56 | ID requested | |
⏵ 1 | 2022-08-08 07:23:07 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Structural proteomics, Cryo-EM, Molecular Dynamics, Lysine acetylation, acylation, protein complex stability |
Contact List
Richard Scheltema |
contact affiliation | Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands Netherlands Proteomics Centre, Padualaan 8, 3584 CH Utrecht, The Netherlands |
contact email | R.A.Scheltema@uu.nl |
lab head | |
Pascal Albanese |
contact affiliation | Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands |
contact email | p.albanese@uu.nl |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD035847
- Label: PRIDE project
- Name: Thriving in the heat – Lysine acetylation stabilizes the quaternary structure of a Mega-Dalton hyperthermoactive PEP-synthase