{"_id":"1970","doi":"10.1038/nature09066","month":"05","title":"The architecture of respiratory complex I","issue":"7297","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>","short":"R. Efremov, R. Baradaran, L.A. Sazanov, Nature 465 (2010) 441–445.","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>.","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>.","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.","ista":"Efremov R, Baradaran R, Sazanov LA. 2010. The architecture of respiratory complex I. Nature. 465(7297), 441–445.","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>"},"type":"journal_article","publisher":"Nature Publishing Group","volume":465,"publication_status":"published","acknowledgement":"This work was funded by the Medical Research Council.","publist_id":"5113","author":[{"last_name":"Efremov","first_name":"Rouslan","full_name":"Efremov, Rouslan G"},{"full_name":"Baradaran, Rozbeh ","first_name":"Rozbeh","last_name":"Baradaran"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov","full_name":"Leonid Sazanov","first_name":"Leonid A","orcid":"0000-0002-0977-7989"}],"extern":1,"page":"441 - 445","publication":"Nature","intvolume":"       465","date_updated":"2021-01-12T06:54:25Z","date_created":"2018-12-11T11:54:58Z","abstract":[{"lang":"eng","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."}],"status":"public","year":"2010","day":"27","quality_controlled":0,"date_published":"2010-05-27T00:00:00Z"}