[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 120, Year 2021
Publish dateJan 5, 2021
AuthorsAlexander Mühleip / Rasmus Kock Flygaard / Jana Ovciarikova / Alice Lacombe / Paula Fernandes / Lilach Sheiner / Alexey Amunts /
PubMed AbstractMitochondrial 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 ...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. 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.
External linksNat Commun / PubMed:33402698 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution2.8 - 34.0 Å
Structure data

EMDB-10520: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, membrane region map
PDB-6tmg: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, membrane region model
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-10521: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, OSCP/F1/c-ring map
PDB-6tmh: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, OSCP/F1/c-ring model
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-10522: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, peripheral stalk map
PDB-6tmi: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, peripheral stalk model
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-10523: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, rotor-stator map
PDB-6tmj: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, rotor-stator model
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-10524: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, consensus map
PDB-6tmk: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase dimer, composite model
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-10525: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase hexamer, membrane region
PDB-6tml: Cryo-EM structure of Toxoplasma gondii mitochondrial ATP synthase hexamer, composite model
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-10526:
Subtomogram average of ATP synthase dimer from Toxoplasma gondii mitochondrial membranes
Method: EM (subtomogram averaging) / Resolution: 20.0 Å

EMDB-10527:
Subtomogram average of the ATP synthase dimer from Toxoplasma gondii mitochondria
Method: EM (subtomogram averaging) / Resolution: 34.0 Å

EMDB-11403:
Subtomogram average of the ATP synthase dimer from Toxoplasma gondii ATPTG11-KO mitochondrial membranes
Method: EM (subtomogram averaging) / Resolution: 22.0 Å

Chemicals

ChemComp-PC1:
1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM / Discrete optimized protein energy

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • toxoplasma gondii gt1 (eukaryote)
  • toxoplasma gondii (strain atcc 50853 / gt1) (eukaryote)
KeywordsMEMBRANE PROTEIN / mitochondrial / ATP synthase / membrane region / lipids / F1 / c-ring / peripheral stalk / OSCP / rotor / stator / dimer / hexamer

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more