The architecture of respiratory complex I View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2010-05-27

AUTHORS

Rouslan G. Efremov, Rozbeh Baradaran, Leonid A. Sazanov

ABSTRACT

Complex I is the first enzyme of the respiratory chain and has a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation by an unknown mechanism. Dysfunction of complex I has been implicated in many human neurodegenerative diseases. We have determined the structure of its hydrophilic domain previously. Here, we report the α-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 Å resolution. The antiporter-like subunits NuoL/M/N each contain 14 conserved transmembrane (TM) helices. Two of them are discontinuous, as in some transporters. Unexpectedly, subunit NuoL also contains a 110-Å long amphipathic α-helix, spanning almost the entire length of the domain. Furthermore, we have determined the structure of the entire complex I from Thermus thermophilus at 4.5 Å resolution. The L-shaped assembly consists of the α-helical model for the membrane domain, with 63 TM helices, and the known structure of the hydrophilic domain. The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic α-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation. More... »

PAGES

441-445

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature09066

DOI

http://dx.doi.org/10.1038/nature09066

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050145385

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/20505720


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