Difference between revisions of "Efremov 2011 Nature"
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{{Publication | {{Publication | ||
|title=Efremov RG, Sazanov LA (2011) Structure of the membrane domain of respiratory complex I. Nature 476:414-20. doi | |title=Efremov RG, Sazanov LA (2011) Structure of the membrane domain of respiratory complex I. Nature 476:414-20. https://doi.org/10.1038/nature10330 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/21822288/ PMID: 21822288] | |info=[https://pubmed.ncbi.nlm.nih.gov/21822288/ PMID: 21822288] | ||
|authors=Efremov RG, Sazanov Leonid A | |authors=Efremov RG, Sazanov Leonid A |
Latest revision as of 20:08, 6 November 2023
Efremov RG, Sazanov LA (2011) Structure of the membrane domain of respiratory complex I. Nature 476:414-20. https://doi.org/10.1038/nature10330 |
Efremov RG, Sazanov Leonid A (2011) Nature
Abstract: 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 Γ 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.
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Enzyme: Complex I