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The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates
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Iwata, M., Lee, Y., Yamashita, T., Yagi, T., Iwata, So, Cameron, Alexander and Maher, M. J. (2012) The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates. Proceedings of the National Academy of Sciences, Vol. 109 (No. 38). pp. 15247-15252. doi:10.1073/pnas.1210059109 ISSN 0027-8424.
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Official URL: http://dx.doi.org/10.1073/pnas.1210059109
Abstract
Bioenergy is efficiently produced in the mitochondria by the respiratory system consisting of complexes I–V. In various organisms, complex I can be replaced by the alternative NADH-quinone oxidoreductase (NDH-2), which catalyzes the transfer of an electron from NADH via FAD to quinone, without proton pumping. The Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix. A number of studies have investigated the potential use of Ndi1 as a therapeutic agent against complex I disorders, and the NDH-2 enzymes have emerged as potential therapeutic targets for treatments against the causative agents of malaria and tuberculosis. Here we present the crystal structures of Ndi1 in its substrate-free, NAD+- and ubiquinone- (UQ2) complexed states. The structures reveal that Ndi1 is a peripheral membrane protein forming an intimate dimer, in which packing of the monomeric units within the dimer creates an amphiphilic membrane-anchor domain structure. Crucially, the structures of the Ndi1–NAD+ and Ndi1–UQ2 complexes show overlapping binding sites for the NAD+ and quinone substrates.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Proceedings of the National Academy of Sciences | ||||
Publisher: | National Academy of Sciences | ||||
ISSN: | 0027-8424 | ||||
Official Date: | 2012 | ||||
Dates: |
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Volume: | Vol. 109 | ||||
Number: | No. 38 | ||||
Page Range: | pp. 15247-15252 | ||||
DOI: | 10.1073/pnas.1210059109 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published |
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