PXD013530
PXD013530 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-FO coupling |
Description | F1FO-ATP synthases play a central role in cellular metabolism, making the energy of the protonmotive force across a membrane available for a large number of energy-consuming processes. We determined the single-particle cryo-EM structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at 2.7- 2.8 Å resolution. Separation of 13 well-defined rotary substates by 3D classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30° of each 120° primary rotary step. The joint movement facilitates flexible coupling of the stoichiometrically mismatched F1 and FO subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit, a well-established target of physiologically important inhibitors. Our maps provide atomic detail of the c-ring/a-subunit interface in the membrane, where protonation and deprotonation of c-ring cGlu111 drives rotary catalysis. An essential histidine residue in the lumenal proton access channel binds a strong non-peptide density assigned to a metal ion that may facilitate c-ring protonation, as its coordination geometry changes with c-ring rotation. We resolve ordered water molecules in the proton access and release channels and at the gating aArg239 that is critical in all rotary ATPases. We identify the previously unknown ASA10 subunit and present complete de novo atomic models of subunits ASA1-10, which make up the two interlinked peripheral stalks that stabilize the Polytomella ATP synthase dimer. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:56:21.951.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Julian Langer |
SpeciesList | scientific name: Polytomella parva; NCBI TaxID: 51329; |
ModificationList | acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive; LTQ Orbitrap Elite |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2019-04-16 09:02:17 | ID requested | |
1 | 2019-05-01 08:16:27 | announced | |
2 | 2019-06-27 02:02:20 | announced | Updated publication reference for PubMed record(s): 31221832. |
⏵ 3 | 2024-10-22 04:56:25 | announced | 2024-10-22: Updated project metadata. |
Publication List
Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz Ö, K, ü, hlbrandt W, coupling. Science, 364(6446):(2019) [pubmed] |
10.1126/science.aaw9128; |
Keyword List
submitter keyword: proteomics,ATP Synthase, Electron microscopy, Polytomella |
Contact List
Julian Langer | |
---|---|
contact affiliation | MPI of Biophysics and Brain Research |
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 |
Full Dataset Link List
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PRIDE project URI |
Repository Record List
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