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Structure paper

TitleStructure of Mammalian Respiratory Supercomplex IIIIIV.
Journal, issue, pagesCell, Vol. 167, Issue 6, Page 1598-1609.e10, Year 2016
Publish dateDec 1, 2016
AuthorsMeng Wu / Jinke Gu / Runyu Guo / Yushen Huang / Maojun Yang /
PubMed AbstractThe mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to ...The mammalian respiratory chain complexes assemble into supercomplexes (SCs) and reside in the inner mitochondrial membrane to transfer electrons and establish the proton gradient for complex V to synthesize ATP. The precise arrangement of SCs is largely unknown. Here, we report a 4.0-Å cryo-electron microscopy (cryo-EM) structure of the major SC in porcine heart, the 1.7-MDa SCIIIIIV. The complex III (CIII) dimer and complex IV (CIV) bind at the same side of the L-shaped complex I (CI). Several accessory or supernumerary subunits of CI, such as NDUFA11, NDUFB4, NDUFB8, and NDUFB9, directly contribute to the oligomerization of CI, CIII, and CIV. COX7C and COX7A of CIV attach CIV to the concave surface formed by CIII and the distal end of membrane arm of CI. The structure suggests a possible mechanism by which electrons are transferred from NADH to cytochrome c and provides a platform for future functional dissection of respiration.
External linksCell / PubMed:27912063
MethodsEM (single particle)
Resolution3.38 - 4.0 Å
Structure data

EMDB-6718:
Cryo-EM structure of mammalian respiratory complex III2IV1 by subregion refinement
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-6719:
Cryo-EM structure of mammalian respiratory complex I matrix arm
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-6720:
Cryo-EM structure of mammalian respiratory complex I
Method: EM (single particle) / Resolution: 3.62 Å

9539

5gup

EMDB-9539, PDB-5gup:
Cryo-EM structure of mammalian respiratory supercomplex I1III2IV1
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-PLX:
(9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL / phospholipid*YM

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

ChemComp-ZMP:
S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl] tetradecanethioate

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

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

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-HEC:
HEME C / Heme C

ChemComp-HEA:
HEME-A / Heme A

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • sus scrofa (pig)
  • Pig (pig)
KeywordsELECTRON TRANSPORT / Cryo-EM / Mammalian / Respiratory / Supercomplex

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