{"_id":"1973","status":"public","publisher":"Nature Publishing Group","publication":"Nature","volume":476,"acknowledgement":"This work was funded by the Medical Research Council.","issue":"7361","year":"2011","page":"414 - 421","date_updated":"2021-01-12T06:54:26Z","quality_controlled":0,"publication_status":"published","day":"25","type":"journal_article","author":[{"first_name":"Rouslan","last_name":"Efremov","full_name":"Efremov, Rouslan G"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","first_name":"Leonid A","last_name":"Sazanov","orcid":"0000-0002-0977-7989","full_name":"Leonid Sazanov"}],"month":"08","title":"Structure of the membrane domain of respiratory complex i","intvolume":"       476","extern":1,"citation":{"short":"R. Efremov, L.A. Sazanov, Nature 476 (2011) 414–421.","mla":"Efremov, Rouslan, and Leonid A. Sazanov. “Structure of the Membrane Domain of Respiratory Complex I.” <i>Nature</i>, vol. 476, no. 7361, Nature Publishing Group, 2011, pp. 414–21, doi:<a href=\"https://doi.org/10.1038/nature10330\">10.1038/nature10330</a>.","chicago":"Efremov, Rouslan, and Leonid A Sazanov. “Structure of the Membrane Domain of Respiratory Complex I.” <i>Nature</i>. Nature Publishing Group, 2011. <a href=\"https://doi.org/10.1038/nature10330\">https://doi.org/10.1038/nature10330</a>.","ista":"Efremov R, Sazanov LA. 2011. Structure of the membrane domain of respiratory complex i. Nature. 476(7361), 414–421.","ieee":"R. Efremov and L. A. Sazanov, “Structure of the membrane domain of respiratory complex i,” <i>Nature</i>, vol. 476, no. 7361. Nature Publishing Group, pp. 414–421, 2011.","apa":"Efremov, R., &#38; Sazanov, L. A. (2011). Structure of the membrane domain of respiratory complex i. <i>Nature</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nature10330\">https://doi.org/10.1038/nature10330</a>","ama":"Efremov R, Sazanov LA. Structure of the membrane domain of respiratory complex i. <i>Nature</i>. 2011;476(7361):414-421. doi:<a href=\"https://doi.org/10.1038/nature10330\">10.1038/nature10330</a>"},"date_published":"2011-08-25T00:00:00Z","abstract":[{"text":"Complex I is the first and largest enzyme of the respiratory chain, coupling electron transfer between NADH and ubiquinone to the translocation of four protons across the membrane. It has a central role in cellular energy production and has been implicated in many human neurodegenerative diseases. The L-shaped enzyme consists of hydrophilic and membrane domains. Previously, we determined the structure of the hydrophilic domain. Here we report the crystal structure of the Esherichia coli complex I membrane domain at 3.0 Ã. resolution. It includes six subunits, NuoL, NuoM, NuoN, NuoA, NuoJ and NuoK, with 55 transmembrane helices. The fold of the homologous antiporter-like subunits L, M and N is novel, with two inverted structural repeats of five transmembrane helices arranged, unusually, face-to-back. Each repeat includes a discontinuous transmembrane helix and forms half of a channel across the membrane. A network of conserved polar residues connects the two half-channels, completing the proton translocation pathway. Unexpectedly, lysines rather than carboxylate residues act as the main elements of the proton pump in these subunits. The fourth probable proton-translocation channel is at the interface of subunits N, K, J and A. The structure indicates that proton translocation in complex I, uniquely, involves coordinated conformational changes in six symmetrical structural elements.","lang":"eng"}],"doi":"10.1038/nature10330","publist_id":"5110","date_created":"2018-12-11T11:54:59Z"}