Difference between revisions of "Baradaran 2013 Nature"
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|title=Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494:443-8. doi | |title=Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494:443-8. https://doi.org/10.1038/nature11871 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/23417064/ PMID: 23417064 Open Access] | |info=[https://pubmed.ncbi.nlm.nih.gov/23417064/ PMID: 23417064 Open Access] | ||
|authors=Baradaran R, Berrisford JM, Minhas GS, Sazanov Leonid A | |authors=Baradaran R, Berrisford JM, Minhas GS, Sazanov Leonid A |
Latest revision as of 20:08, 6 November 2023
Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494:443-8. https://doi.org/10.1038/nature11871 |
Baradaran R, Berrisford JM, Minhas GS, Sazanov Leonid A (2013) Nature
Abstract: 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 Γ 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.
β’ Bioblast editor: Gnaiger E
Labels:
Enzyme: Complex I Regulation: Coupling efficiency;uncoupling