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Structure paper

TitleA Dynamic Substrate Pool Revealed by cryo-EM of a Lipid-Preserved Respiratory Supercomplex.
Journal, issue, pagesAntioxid Redox Signal, Year 2022
Publish dateApr 27, 2022
AuthorsTae Jin Jeon / Seong-Gyu Lee / Suk Hyun Yoo / Myeongbin Kim / Dabin Song / Joonghyun Ryu / Hwangseo Park / Deok-Soo Kim / Jaekyung Hyun / Ho Min Kim / Seong Eon Ryu /
PubMed Abstract Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in ... Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in physiologically relevant conditions, we conducted cryoelectron microscopy studies with supercomplexes in a lipid-preserving state. Here, we present cryoelectron microscopy structures of bovine respiratory supercomplex IIIIIV by using a lipid-preserving sample preparation. The preparation greatly enhances the intercomplex quinone transfer activity. The structures reveal large intercomplex motions that result in different shapes and sizes of the intercomplex space between complexes I and III, forming a dynamic substrate pool. Biochemical and structural analyses indicated that intercomplex phospholipids mediate the intercomplex motions. An analysis of the different classes of focus-refined complex I showed that structural switches due to quinone reduction led to the formation of a novel channel that could transfer reduced quinones to the intercomplex substrate pool. Our results indicate potential mechanism for the facilitated electron transfer involving a dynamic substrate pool and intercomplex movement by which supercomplexes play an active role in the regulation of metabolic flux and reactive oxygen species.
External linksAntioxid Redox Signal / PubMed:34913730
MethodsEM (single particle)
Resolution3.8 - 8.3 Å
Structure data

30673

7dgq

EMDB-30673, PDB-7dgq:
Activity optimized supercomplex state1
Method: EM (single particle) / Resolution: 5.0 Å

30674

7dgr

EMDB-30674, PDB-7dgr:
Activity optimized supercomplex state2
Method: EM (single particle) / Resolution: 4.6 Å

30675

7dgs

EMDB-30675, PDB-7dgs:
Activity optimized supercomplex state3
Method: EM (single particle) / Resolution: 7.8 Å

30676

7dgz

EMDB-30676, PDB-7dgz:
Activity optimized complex I (closed form)
Method: EM (single particle) / Resolution: 3.8 Å

30677

7dh0

EMDB-30677, PDB-7dh0:
Activity optimized complex I (open form)
Method: EM (single particle) / Resolution: 4.2 Å

30706

7dkf

EMDB-30706, PDB-7dkf:
Activity optimized supercomplex state4
Method: EM (single particle) / Resolution: 8.3 Å

Chemicals

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

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

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

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE / Flavin mononucleotide

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

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-HEA:
HEME-A / Heme A

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-HEC:
HEME C / Heme C

ChemComp-UQ2:
UBIQUINONE-2

Source
  • bos taurus (cattle)
  • Bovine (cattle)
KeywordsOXIDOREDUCTASE / respiratory / electron transport / Complex I

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