Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans.

TitleTruncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans.
Publication TypeJournal Article
Year of Publication2010
AuthorsBirrell, JA, Hirst, J
JournalFEBS Lett
Volume584
Issue19
Pagination4247-52
Date Published2010 Oct 08
ISSN1873-3468
KeywordsAmino Acid Sequence, Animals, Arabidopsis, Caenorhabditis elegans, Cattle, Chondrus, Electron Transport Complex I, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Sequence Homology, Amino Acid, Thermus thermophilus, Yarrowia
Abstract

Three of the conserved, membrane-bound subunits in NADH:ubiquinone oxidoreductase (complex I) are related to one another, and to Mrp sodium-proton antiporters. Recent structural analysis of two prokaryotic complexes I revealed that the three subunits each contain fourteen transmembrane helices that overlay in structural alignments: the translocation of three protons may be coordinated by a lateral helix connecting them together (Efremov, R.G., Baradaran, R. and Sazanov, L.A. (2010). The architecture of respiratory complex I. Nature 465, 441-447). Here, we show that in higher metazoans the threefold symmetry is broken by the loss of three helices from subunit ND2; possible implications for the mechanism of proton translocation are discussed.

DOI10.1016/j.febslet.2010.09.017
Alternate JournalFEBS Lett.
Citation Key10.1016/j.febslet.2010.09.017
PubMed ID20846527
Grant List / / Medical Research Council / United Kingdom