{"type":"journal_article","extern":1,"volume":465,"date_updated":"2021-01-12T06:54:25Z","publist_id":"5113","intvolume":"       465","title":"The architecture of respiratory complex I","quality_controlled":0,"author":[{"last_name":"Efremov","full_name":"Efremov, Rouslan G","first_name":"Rouslan"},{"last_name":"Baradaran","first_name":"Rozbeh","full_name":"Baradaran, Rozbeh "},{"last_name":"Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Leonid Sazanov","first_name":"Leonid A","orcid":"0000-0002-0977-7989"}],"doi":"10.1038/nature09066","_id":"1970","abstract":[{"text":"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 α-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 Å 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-Å long amphipathic α-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 Å resolution. The L-shaped assembly consists of the α-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 α-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation.","lang":"eng"}],"publication_status":"published","issue":"7297","publication":"Nature","acknowledgement":"This work was funded by the Medical Research Council.","date_created":"2018-12-11T11:54:58Z","month":"05","citation":{"apa":"Efremov, R., Baradaran, R., &#38; Sazanov, L. A. (2010). The architecture of respiratory complex I. <i>Nature</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nature09066\">https://doi.org/10.1038/nature09066</a>","chicago":"Efremov, Rouslan, Rozbeh Baradaran, and Leonid A Sazanov. “The Architecture of Respiratory Complex I.” <i>Nature</i>. Nature Publishing Group, 2010. <a href=\"https://doi.org/10.1038/nature09066\">https://doi.org/10.1038/nature09066</a>.","ista":"Efremov R, Baradaran R, Sazanov LA. 2010. The architecture of respiratory complex I. Nature. 465(7297), 441–445.","ieee":"R. Efremov, R. Baradaran, and L. A. Sazanov, “The architecture of respiratory complex I,” <i>Nature</i>, vol. 465, no. 7297. Nature Publishing Group, pp. 441–445, 2010.","ama":"Efremov R, Baradaran R, Sazanov LA. The architecture of respiratory complex I. <i>Nature</i>. 2010;465(7297):441-445. doi:<a href=\"https://doi.org/10.1038/nature09066\">10.1038/nature09066</a>","mla":"Efremov, Rouslan, et al. “The Architecture of Respiratory Complex I.” <i>Nature</i>, vol. 465, no. 7297, Nature Publishing Group, 2010, pp. 441–45, doi:<a href=\"https://doi.org/10.1038/nature09066\">10.1038/nature09066</a>.","short":"R. Efremov, R. Baradaran, L.A. Sazanov, Nature 465 (2010) 441–445."},"day":"27","page":"441 - 445","year":"2010","publisher":"Nature Publishing Group","status":"public","date_published":"2010-05-27T00:00:00Z"}