Structure of the membrane domain of respiratory complex I

Efremov, Rouslan G.; Sazanov, Leonid A.

doi:10.1038/nature10330

Cited by 370Enzyme Structure and FunctionMitochondrial Function and PathologyATP Synthase and ATPases Research

Structure of the membrane domain of respiratory complex I

Efremov, Rouslan G., Sazanov, Leonid A.·2011·Nature

DOI 10.1038/nature10330

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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 Å 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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Authors: Efremov, R. G., & Sazanov, L. A.
Affiliations: Max Planck Institute of Molecular Physiology (DE)
MRC Mitochondrial Biology Unit (GB)
Corresponding author: Sazanov, Leonid A.
ORCID: Efremov, Rouslan G.
Sazanov, Leonid A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2011-08
Volume: 476
Issue: 7361
Pages: 414-420
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature10330
OpenAlex: W1987127397
Cited by: 370
References: 64
Citations by year: 2026: 8 · 2025: 7 · 2024: 15 · 2023: 8 · 2022: 22 · 2021: 21 · 2020: 21 · 2019: 18 · 2018: 25 · 2017: 22 · 2016: 31 · 2015: 36 · 2014: 39 · 2013: 39 · 2012: 50
FWCI: 21.32
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
DORA PSI (Paul Scherrer Institute) (submittedVersion)
Max Planck Institute for Plasma Physics (submittedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
Funders: European Synchrotron Radiation Facility
Medical Research Council
Topics: Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: mitochondrial complex I, membrane domains, crystal structure, proton translocation, proton pump, lysine residues, transmembrane helices, Escherichia coli, neurodegenerative diseases
MeSH terms: Cell Membrane, Escherichia coli, Lysine, Models, Molecular, NAD, NADH Dehydrogenase, Protein Binding, Protons, Ubiquinone, Ion Transport, Protein Structure, Tertiary, Protein Folding, Antiporters, Crystallography, X-Ray, Protein Subunits, Escherichia coli Proteins, Electron Transport Complex I

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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Structure of the membrane domain of respiratory complex I

Abstract

Integrity signals

Claims the paper makes

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Cites

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