PXD013530

PXD013530 is an original dataset announced via ProteomeXchange.

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

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.

Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz Ö, K, ü, hlbrandt W, coupling. Science, 364(6446):(2019) [pubmed]

10.1126/science.aaw9128;

submitter keyword: proteomics,ATP Synthase, Electron microscopy, Polytomella

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

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/2019/05/PXD013530

PRIDE project URI

• PRIDE
  1. PXD013530
     1. Label: PRIDE project
     2. Name: Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-FO coupling