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TitleStructure of the intact 14-subunit human cytochrome c oxidase.
Journal, issue, pagesCell Res, Vol. 28, Issue 10, Page 1026-1034, Year 2018
Publish dateJul 20, 2018
AuthorsShuai Zong / Meng Wu / Jinke Gu / Tianya Liu / Runyu Guo / Maojun Yang /
PubMed AbstractRespiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria. Complex-IV is the ...Respiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria. Complex-IV is the terminal enzyme of the electron transport chain, existing either as randomly scattered complexes or as a component of supercomplexes. NDUFA4 was previously assumed as a subunit of complex-I, but recent biochemical data suggested it may be a subunit of complex-IV. However, no structural evidence supporting this notion was available till now. Here we obtained the 3.3 Å resolution structure of complex-IV derived from the human supercomplex IIIIIV and assigned the NDUFA4 subunit into complex-IV. Intriguingly, NDUFA4 lies exactly at the dimeric interface observed in previously reported crystal structures of complex-IV homodimer which would preclude complex-IV dimerization. Combining previous structural and biochemical data shown by us and other groups, we propose that the intact complex-IV is a monomer containing 14 subunits.
External linksCell Res / PubMed:30030519 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

6896

5z62

EMDB-6896, PDB-5z62:
Structure of human cytochrome c oxidase
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-MG:
Unknown entry

ChemComp-HEA:
HEME-A / Heme A

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

ChemComp-CDL:
CARDIOLIPIN / phospholipid*YM / Cardiolipin

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsELECTRON TRANSPORT / cytochrome c oxidase

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