{"acknowledgement":"Funded by      Health Research Council of New Zealand     Royal Society of New Zealand     University of Otago     New Zealand Synchrotron Group","citation":{"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.","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>","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>.","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.","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>","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.","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>."},"month":"03","date_created":"2018-12-11T11:55:01Z","year":"2014","publisher":"Wiley-Blackwell","status":"public","page":"950 - 964","day":"01","date_published":"2014-03-01T00:00:00Z","date_updated":"2021-01-12T06:54:29Z","publist_id":"5103","volume":91,"extern":1,"type":"journal_article","intvolume":"        91","_id":"1980","doi":"10.1111/mmi.12507","author":[{"first_name":"Adam","full_name":"Heikal, Adam ","last_name":"Heikal"},{"last_name":"Nakatani","first_name":"Yoshio","full_name":"Nakatani, Yoshio"},{"last_name":"Dunn","first_name":"Elyse","full_name":"Dunn, Elyse A"},{"last_name":"Weimar","first_name":"Marion","full_name":"Weimar, Marion R"},{"first_name":"Catherine","full_name":"Day, Catherine","last_name":"Day"},{"last_name":"Baker","first_name":"Edward","full_name":"Baker, Edward N"},{"full_name":"Lott, Shaun J","first_name":"Shaun","last_name":"Lott"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov","orcid":"0000-0002-0977-7989","first_name":"Leonid A","full_name":"Leonid Sazanov"},{"last_name":"Cook","first_name":"Gregory","full_name":"Cook, Gregory"}],"quality_controlled":0,"title":"Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation","publication":"Molecular Microbiology","publication_status":"published","issue":"5","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"}]}