[{"publication":"Molecular Microbiology","fulldoi":"https://doi.org/10.1111/mmi.12507","publication_status":"published","publist_id":"5103","type":"journal_article","issue":"5","status":"public","year":"2014","extern":"1","intvolume":"        91","date_published":"2014-03-01T00:00:00Z","date_created":"2018-12-11T11:55:01Z","page":"950 - 964","day":"01","author":[{"last_name":"Heikal","full_name":"Heikal, Adam","first_name":"Adam"},{"first_name":"Yoshio","full_name":"Nakatani, Yoshio","last_name":"Nakatani"},{"first_name":"Elyse","full_name":"Dunn, Elyse","last_name":"Dunn"},{"last_name":"Weimar","first_name":"Marion","full_name":"Weimar, Marion"},{"first_name":"Catherine","full_name":"Day, Catherine","last_name":"Day"},{"last_name":"Baker","full_name":"Baker, Edward","first_name":"Edward"},{"first_name":"Shaun","full_name":"Lott, Shaun","last_name":"Lott"},{"first_name":"Leonid A","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989","last_name":"Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Cook, Gregory","first_name":"Gregory","last_name":"Cook"}],"pmid":1,"article_type":"original","OA_type":"free access","volume":91,"publication_identifier":{"issn":["0950-382X"],"eissn":["1365-2958"]},"abstract":[{"text":"Non-proton pumping type II NADH dehydrogenase (NDH-2) plays a central role in the respiratory metabolism of bacteria, and in the mitochondria of fungi, plants and protists. The lack of NDH-2 in mammalian mitochondria and its essentiality in important bacterial pathogens suggests these enzymes may represent a potential new drug target to combat microbial pathogens. Here, we report the first crystal structure of a bacterial NDH-2 enzyme at 2.5Å resolution from Caldalkalibacillus thermarum. The NDH-2 structure reveals a homodimeric organization that has a unique dimer interface. NDH-2 is localized to the cytoplasmic membrane by two separated C-terminal membrane-anchoring regions that are essential for membrane localization and FAD binding, but not NDH-2 dimerization. Comparison of bacterial NDH-2 with the yeast NADH dehydrogenase (Ndi1) structure revealed non-overlapping binding sites for quinone and NADH in the bacterial enzyme. The bacterial NDH-2 structure establishes a framework for the structure-based design of small-molecule inhibitors.","lang":"eng"}],"citation":{"short":"A. Heikal, Y. Nakatani, E. Dunn, M. Weimar, C. Day, E. Baker, S. Lott, L.A. Sazanov, G. Cook, Molecular Microbiology 91 (2014) 950–964.","chicago":"Heikal, Adam, Yoshio Nakatani, Elyse Dunn, Marion Weimar, Catherine Day, Edward Baker, Shaun Lott, Leonid A Sazanov, and Gregory Cook. “Structure of the Bacterial Type II NADH Dehydrogenase: A Monotopic Membrane Protein with an Essential Role in Energy Generation.” <i>Molecular Microbiology</i>. Wiley-Blackwell, 2014. <a href=\"https://doi.org/10.1111/mmi.12507\">https://doi.org/10.1111/mmi.12507</a>.","ama":"Heikal A, Nakatani Y, Dunn E, et al. Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. <i>Molecular Microbiology</i>. 2014;91(5):950-964. doi:<a href=\"https://doi.org/10.1111/mmi.12507\">10.1111/mmi.12507</a>","ieee":"A. Heikal <i>et al.</i>, “Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation,” <i>Molecular Microbiology</i>, vol. 91, no. 5. Wiley-Blackwell, pp. 950–964, 2014.","ista":"Heikal A, Nakatani Y, Dunn E, Weimar M, Day C, Baker E, Lott S, Sazanov LA, Cook G. 2014. Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. Molecular Microbiology. 91(5), 950–964.","mla":"Heikal, Adam, et al. “Structure of the Bacterial Type II NADH Dehydrogenase: A Monotopic Membrane Protein with an Essential Role in Energy Generation.” <i>Molecular Microbiology</i>, vol. 91, no. 5, Wiley-Blackwell, 2014, pp. 950–64, doi:<a href=\"https://doi.org/10.1111/mmi.12507\">10.1111/mmi.12507</a>.","apa":"Heikal, A., Nakatani, Y., Dunn, E., Weimar, M., Day, C., Baker, E., … Cook, G. (2014). Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation. <i>Molecular Microbiology</i>. Wiley-Blackwell. <a href=\"https://doi.org/10.1111/mmi.12507\">https://doi.org/10.1111/mmi.12507</a>"},"doi":"10.1111/mmi.12507","article_processing_charge":"No","external_id":{"pmid":["24444429"]},"acknowledgement":"Funded by      Health Research Council of New Zealand     Royal Society of New Zealand     University of Otago     New Zealand Synchrotron Group","date_updated":"2026-09-04T11:27:46Z","_id":"1980","publisher":"Wiley-Blackwell","title":"Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation","oa_version":"None","language":[{"iso":"eng"}],"month":"03","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345"}]