[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

TitleStructures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMar 17, 2026
AuthorsAtsuki Nakano / Takahiro Masuya / Shinsuke Akisada / Moe Ishikawa-Fukuda / Kaoru Mitsuoka / Hideto Miyoshi / Masatoshi Murai / Ken Yokoyama /
PubMed AbstractUnderstanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the ...Understanding the functional mechanisms of membrane protein complexes requires structural analysis within their native membrane environment. Here, we applied cryo-electron microscopy to determine the structures of FF ATP synthase and respiratory supercomplexes (SCs) on sub-mitochondrial particles (SMPs) isolated from bovine heart mitochondria. Most FF complexes were observed as dimers stabilized by the regulatory factor IF₁, and a tetrameric assembly comprising two FF-IF₁ dimers arranged linearly was also identified. This finding indicates that the tetrameric units of FF are present in the mitochondrial inner membrane and contribute to shaping cristae tips in mammalian mitochondria. F domain maps resolve the e-subunit- c₈-ring interface and show no discrete density for a tightly bound lipid within the c₈-ring. In addition to the previously reported SCs compositions CI₁CIII₂CIV₁ and CI₁CIII₂CIV₂, our analysis identified an additional assembly with the composition CI₁CIII₂CIV₃, as well as a CI₂CIII₂CIV₆ mega-complex. This approach enables rapid structural determination of FF ATP synthase and SCs from minimal membrane fractions, providing a foundation for elucidating the molecular basis of metabolic disorders and mitochondrial diseases at the level of higher-order architecture.
External linksNat Commun / PubMed:41844608
MethodsEM (single particle)
Resolution2.2 - 4.1 Å
Structure data

EMDB-65577, PDB-9w2r:
Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial particles (FoF1-1)
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-65578, PDB-9w2s:
Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial particles (FoF1-2)
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-65579, PDB-9w2t:
Cryo-EM structure of Fo domain of FoF1-ATPase monomer state on the bovine heart submitochondrial particles
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-65580, PDB-9w2u:
Cryo-EM structure of complex I on the bovine heart submitochondrial particles, open
Method: EM (single particle) / Resolution: 2.6 Å

EMDB-65581, PDB-9w2v:
Cryo-EM structure of complex I on the bovine heart submitochondrial particles, closed
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-65583, PDB-9w2x:
Cryo-EM structure of complex III on the bovine heart submitochondrial particles, III-1
Method: EM (single particle) / Resolution: 2.2 Å

EMDB-65584, PDB-9w2y:
Cryo-EM structure of complex III on the bovine heart submitochondrial particles, III-2
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-65585, PDB-9w2z:
Cryo-EM structure of complex IV on the bovine heart submitochondrial particles, IV-A
Method: EM (single particle) / Resolution: 2.61 Å

EMDB-65586: Cryo-EM structure of complex IV on the bovine heart submitochondrial particles, IV-B
Method: EM (single particle) / Resolution: 2.86 Å

EMDB-65587: Cryo-EM structure of complex IV on the bovine heart submitochondrial particles, IV-C
Method: EM (single particle) / Resolution: 3.98 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

ChemComp-FME:
N-FORMYLMETHIONINE

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

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-K:
Unknown entry

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM

ChemComp-CHD:
CHOLIC ACID

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-ZN:
Unknown entry

ChemComp-MYR:
MYRISTIC ACID

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HEC:
HEME C

ChemComp-HEA:
HEME-A

ChemComp-CU:
COPPER (II) ION

ChemComp-PER:
PEROXIDE ION

ChemComp-PGV:
(1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE / phospholipid*YM

ChemComp-CUA:
DINUCLEAR COPPER ION

ChemComp-NA:
Unknown entry

ChemComp-PEK:
(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,11,14-TETRAENOATE / phospholipid*YM

Source
  • bos taurus (domestic cattle)
KeywordsMOTOR PROTEIN / ATP synthase / FoF1-ATPase / submitochondrial particles / OXIDOREDUCTASE / respiratory chain complex / supercomplex

+
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