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http://purl.uniprot.org/citations/23417064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23417064http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23417064http://www.w3.org/2000/01/rdf-schema#comment"Complex I is the first and largest enzyme of the respiratory chain and has a central role in cellular energy production through the coupling of NADH:ubiquinone electron transfer to proton translocation. It is also implicated in many common human neurodegenerative diseases. Here, we report the first crystal structure of the entire, intact complex I (from Thermus thermophilus) at 3.3 Å resolution. The structure of the 536-kDa complex comprises 16 different subunits, with a total of 64 transmembrane helices and 9 iron-sulphur clusters. The core fold of subunit Nqo8 (ND1 in humans) is, unexpectedly, similar to a half-channel of the antiporter-like subunits. Small subunits nearby form a linked second half-channel, which completes the fourth proton-translocation pathway (present in addition to the channels in three antiporter-like subunits). The quinone-binding site is unusually long, narrow and enclosed. The quinone headgroup binds at the deep end of this chamber, near iron-sulphur cluster N2. Notably, the chamber is linked to the fourth channel by a 'funnel' of charged residues. The link continues over the entire membrane domain as a flexible central axis of charged and polar residues, and probably has a leading role in the propagation of conformational changes, aided by coupling elements. The structure suggests that a unique, out-of-the-membrane quinone-reaction chamber enables the redox energy to drive concerted long-range conformational changes in the four antiporter-like domains, resulting in translocation of four protons per cycle."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.org/dc/terms/identifier"doi:10.1038/nature11871"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.org/dc/terms/identifier"doi:10.1038/nature11871"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Sazanov L.A."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Sazanov L.A."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Berrisford J.M."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Berrisford J.M."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Baradaran R."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Baradaran R."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Minhas G.S."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/author"Minhas G.S."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/pages"443-448"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/pages"443-448"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/title"Crystal structure of the entire respiratory complex I."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/title"Crystal structure of the entire respiratory complex I."xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/volume"494"xsd:string
http://purl.uniprot.org/citations/23417064http://purl.uniprot.org/core/volume"494"xsd:string
http://purl.uniprot.org/citations/23417064http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23417064
http://purl.uniprot.org/citations/23417064http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23417064