6TMI

Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, peripheral stalk model


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.

Muhleip, A.Kock Flygaard, R.Ovciarikova, J.Lacombe, A.Fernandes, P.Sheiner, L.Amunts, A.

(2021) Nat Commun 12: 120-120

  • DOI: https://doi.org/10.1038/s41467-020-20381-z
  • Primary Citation of Related Structures:  
    6TMG, 6TMH, 6TMI, 6TMJ, 6TMK, 6TML

  • PubMed Abstract: 

    Mitochondrial ATP synthase plays a key role in inducing membrane curvature to establish cristae. In Apicomplexa causing diseases such as malaria and toxoplasmosis, an unusual cristae morphology has been observed, but its structural basis is unknown. Here, we report that the apicomplexan ATP synthase assembles into cyclic hexamers, essential to shape their distinct cristae. Cryo-EM was used to determine the structure of the hexamer, which is held together by interactions between parasite-specific subunits in the lumenal region. Overall, we identified 17 apicomplexan-specific subunits, and a minimal and nuclear-encoded subunit-a. The hexamer consists of three dimers with an extensive dimer interface that includes bound cardiolipins and the inhibitor IF 1 . Cryo-ET and subtomogram averaging revealed that hexamers arrange into ~20-megadalton pentagonal pyramids in the curved apical membrane regions. Knockout of the linker protein ATPTG11 resulted in the loss of pentagonal pyramids with concomitant aberrantly shaped cristae. Together, this demonstrates that the unique macromolecular arrangement is critical for the maintenance of cristae morphology in Apicomplexa.


  • Organizational Affiliation

    Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165, Solna, Sweden.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP synthase subunit alphaA [auth C]565Toxoplasma gondii GT1Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for S7UU80 (Toxoplasma gondii (strain ATCC 50853 / GT1))
Explore S7UU80 
Go to UniProtKB:  S7UU80
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupS7UU80
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Oligomycin sensitivity conferring protein (OSCP)B [auth G]252Toxoplasma gondii GT1Mutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for A0A125YKF8 (Toxoplasma gondii (strain ATCC 50853 / GT1))
Explore A0A125YKF8 
Go to UniProtKB:  A0A125YKF8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A125YKF8
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
subunit dC [auth A]536Toxoplasma gondii GT1Mutation(s): 0 
UniProt
Find proteins for S7V493 (Toxoplasma gondii (strain ATCC 50853 / GT1))
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Go to UniProtKB:  S7V493
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UniProt GroupS7V493
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ATPTG12D [auth R]134Toxoplasma gondii GT1Mutation(s): 0 
UniProt
Find proteins for A0A125YKF7 (Toxoplasma gondii (strain ATCC 50853 / GT1))
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Go to UniProtKB:  A0A125YKF7
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UniProt GroupA0A125YKF7
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  • Reference Sequence
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
subunit bE [auth B]571Toxoplasma gondii GT1Mutation(s): 0 
UniProt
Find proteins for S7V2T0 (Toxoplasma gondii (strain ATCC 50853 / GT1))
Explore S7V2T0 
Go to UniProtKB:  S7V2T0
Entity Groups  
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UniProt GroupS7V2T0
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX1.17rc2-3612
RECONSTRUCTIONRELION3.0

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swedish Research CouncilSwedenNT_2015-04107
European Research CouncilSwedenERC-2018-StG-805230
Knut and Alice Wallenberg FoundationSweden2018.0080
European Molecular Biology OrganizationSwedenALTF 260-2017

Revision History  (Full details and data files)

  • Version 1.0: 2020-12-16
    Type: Initial release
  • Version 1.1: 2021-01-20
    Changes: Database references
  • Version 1.2: 2024-05-22
    Changes: Data collection, Database references