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http://purl.uniprot.org/citations/30030519http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30030519http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30030519http://www.w3.org/2000/01/rdf-schema#comment"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 I1III2IV1 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."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.org/dc/terms/identifier"doi:10.1038/s41422-018-0071-1"xsd:string
http://purl.uniprot.org/citations/30030519http://purl.org/dc/terms/identifier"doi:10.1038/s41422-018-0071-1"xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Guo R."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Guo R."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Gu J."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Gu J."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Liu T."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Liu T."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Wu M."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Wu M."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Yang M."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Zong S."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/author"Zong S."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/name"Cell Res."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/name"Cell Res."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/pages"1026-1034"xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/pages"1026-1034"xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/title"Structure of the intact 14-subunit human cytochrome c oxidase."xsd:string
http://purl.uniprot.org/citations/30030519http://purl.uniprot.org/core/title"Structure of the intact 14-subunit human cytochrome c oxidase."xsd:string