Efremov 2010 Nature: Difference between revisions
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{{Publication | {{Publication | ||
|title=Efremov RG, Baradaran R, Sazanov LA (2010) The architecture of respiratory complex I. Nature 465:441-5. doi | |title=Efremov RG, Baradaran R, Sazanov LA (2010) The architecture of respiratory complex I. Nature 465:441-5. https://doi.org/10.1038/nature09066 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/20505720/ PMID: 20505720] | |info=[https://pubmed.ncbi.nlm.nih.gov/20505720/ PMID: 20505720] | ||
|authors=Efremov RG, Baradaran R, Sazanov Leonid A | |authors=Efremov RG, Baradaran R, Sazanov Leonid A |
Latest revision as of 20:08, 6 November 2023
Efremov RG, Baradaran R, Sazanov LA (2010) The architecture of respiratory complex I. Nature 465:441-5. https://doi.org/10.1038/nature09066 |
Efremov RG, Baradaran R, Sazanov Leonid A (2010) Nature
Abstract: Complex I is the first enzyme of the respiratory chain and has a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation by an unknown mechanism. Dysfunction of complex I has been implicated in many human neurodegenerative diseases. We have determined the structure of its hydrophilic domain previously. Here, we report the alpha-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 A resolution. The antiporter-like subunits NuoL/M/N each contain 14 conserved transmembrane (TM) helices. Two of them are discontinuous, as in some transporters. Unexpectedly, subunit NuoL also contains a 110-A long amphipathic alpha-helix, spanning almost the entire length of the domain. Furthermore, we have determined the structure of the entire complex I from Thermus thermophilus at 4.5 A resolution. The L-shaped assembly consists of the alpha-helical model for the membrane domain, with 63 TM helices, and the known structure of the hydrophilic domain. The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic alpha-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation.
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Enzyme: Complex I