Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

The architecture of the mammalian respirasome

This article has been updated

Abstract

The respiratory chain complexes I, III and IV (CI, CIII and CIV) are present in the bacterial membrane or the inner mitochondrial membrane and have a role of transferring electrons and establishing the proton gradient for ATP synthesis by complex V. The respiratory chain complexes can assemble into supercomplexes (SCs), but their precise arrangement is unknown. Here we report a 5.4 Å cryo-electron microscopy structure of the major 1.7 megadalton SCI1III2IV1 respirasome purified from porcine heart. The CIII dimer and CIV bind at the same side of the L-shaped CI, with their transmembrane domains essentially aligned to form a transmembrane disk. Compared to free CI, the CI in the respirasome is more compact because of interactions with CIII and CIV. The NDUFA11 and NDUFB9 supernumerary subunits of CI contribute to the oligomerization of CI and CIII. The structure of the respirasome provides information on the precise arrangements of the respiratory chain complexes in mitochondria.

Access options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

Figure 1: Cryo-EM structure of the respirasome.
Figure 2: Assignment of the SCI1III2IV1.
Figure 3: Overall structure of CI.
Figure 4: Interaction between the three complexes.

Accession codes

Primary accessions

Protein Data Bank

Data deposits

The 3D cryo-EM density map has been deposited in the Electron Microscopy Data Bank (EMDB), with accession code EMD- 9534. The coordinates of atomic models have been deposited in the Protein Data Bank (PDB) under the accession code 5GPN for the respirasome.

Change history

  • 28 September 2016

    The reported number of transmembrane helices in the CIII dimer was corrected.

References

  1. 1

    Viscomi, C., Bottani, E. & Zeviani, M. Emerging concepts in the therapy of mitochondrial disease. Biochim. Biophys. Acta 1847, 544–557 (2015)

    CAS  PubMed  Article  Google Scholar 

  2. 2

    Wallace, D. C. Mitochondrial DNA variation in human radiation and disease. Cell 163, 33–38 (2015)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  3. 3

    Wallace, D. C. & Chalkia, D. Mitochondrial DNA genetics and the heteroplasmy conundrum in evolution and disease. Cold Spring Harb. Perspect. Biol. 5, a021220 (2013)

    PubMed  PubMed Central  Article  CAS  Google Scholar 

  4. 4

    Schägger, H. & Pfeiffer, K. The ratio of oxidative phosphorylation complexes I–V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J. Biol. Chem. 276, 37861–37867 (2001)

    PubMed  Google Scholar 

  5. 5

    Lenaz, G. & Genova, M. L. Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject. Antioxid. Redox Signal. 12, 961–1008 (2010)

    CAS  PubMed  Article  Google Scholar 

  6. 6

    Sone, N., Sekimachi, M. & Kutoh, E. Identification and properties of a quinol oxidase super-complex composed of a bc1 complex and cytochrome oxidase in the thermophilic bacterium PS3. J. Biol. Chem. 262, 15386–15391 (1987)

    CAS  PubMed  Google Scholar 

  7. 7

    Berry, E. A. & Trumpower, B. L. Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes. J. Biol. Chem. 260, 2458–2467 (1985)

    CAS  PubMed  Google Scholar 

  8. 8

    Schägger, H. Respiratory chain supercomplexes. IUBMB Life 52, 119–128 (2001)

    PubMed  Article  Google Scholar 

  9. 9

    Schägger, H. & Pfeiffer, K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777–1783 (2000)

    PubMed  PubMed Central  Article  Google Scholar 

  10. 10

    Dudkina, N. V., Eubel, H., Keegstra, W., Boekema, E. J. & Braun, H. P. Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc. Natl Acad. Sci. USA 102, 3225–3229 (2005)

    ADS  CAS  PubMed  Article  Google Scholar 

  11. 11

    Shinzawa-Itoh, K. et al. Purification of active respiratory supercomplex from bovine heart mitochondria enables functional studies. J. Biol. Chem. 291, 4178–4184 (2016)

    CAS  PubMed  Article  Google Scholar 

  12. 12

    Althoff, T., Mills, D. J., Popot, J. L. & Kühlbrandt, W. Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1 . EMBO J. 30, 4652–4664 (2011)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  13. 13

    Schäfer, E., Dencher, N. A., Vonck, J. & Parcej, D. N. Three-dimensional structure of the respiratory chain supercomplex I1III2IV1 from bovine heart mitochondria. Biochemistry 46, 12579–12585 (2007)

    PubMed  Article  CAS  Google Scholar 

  14. 14

    Acín-Pérez, R., Fernández-Silva, P., Peleato, M. L., Pérez-Martos, A. & Enriquez, J. A. Respiratory active mitochondrial supercomplexes. Mol. Cell 32, 529–539 (2008)

    PubMed  Article  CAS  Google Scholar 

  15. 15

    Acín-Pérez, R. et al. Respiratory complex III is required to maintain complex I in mammalian mitochondria. Mol. Cell 13, 805–815 (2004)

    PubMed  PubMed Central  Article  Google Scholar 

  16. 16

    Stroh, A. et al. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 279, 5000–5007 (2004)

    CAS  PubMed  Article  Google Scholar 

  17. 17

    Diaz, F., Fukui, H., Garcia, S. & Moraes, C. T. Cytochrome c oxidase is required for the assembly/stability of respiratory complex I in mouse fibroblasts. Mol. Cell. Biol. 26, 4872–4881 (2006)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  18. 18

    Wittig, I., Carrozzo, R., Santorelli, F. M. & Schägger, H. Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation. Biochim. Biophys. Acta 1757, 1066–1072 (2006)

    CAS  PubMed  Article  Google Scholar 

  19. 19

    Bultema, J. B., Braun, H. P., Boekema, E. J. & Kouril, R. Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato. Biochim. Biophys. Acta 1787, 60–67 (2009)

    CAS  PubMed  Article  Google Scholar 

  20. 20

    Wittig, I. & Schägger, H. Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes. Biochim. Biophys. Acta 1787, 672–680 (2009)

    CAS  PubMed  Article  Google Scholar 

  21. 21

    Dudkina, N. V., Kudryashev, M., Stahlberg, H. & Boekema, E. J. Interaction of complexes I, III, and IV within the bovine respirasome by single particle cryoelectron tomography. Proc. Natl Acad. Sci. USA 108, 15196–15200 (2011)

    ADS  CAS  PubMed  Article  Google Scholar 

  22. 22

    Schäfer, E. et al. Architecture of active mammalian respiratory chain supercomplexes. J. Biol. Chem. 281, 15370–15375 (2006). 10

    PubMed  Article  CAS  Google Scholar 

  23. 23

    Vinothkumar, K. R., Zhu, J. & Hirst, J. Architecture of mammalian respiratory complex I. Nature 515, 80–84 (2014)

    ADS  CAS  PubMed  PubMed Central  Article  Google Scholar 

  24. 24

    Iwata, S. et al. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. Science 281, 64–71 (1998)

    ADS  CAS  PubMed  Article  Google Scholar 

  25. 25

    Tsukihara, T. et al. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 272, 1136–1144 (1996)

    ADS  CAS  Article  Google Scholar 

  26. 26

    Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)

    PubMed  PubMed Central  Article  CAS  Google Scholar 

  27. 27

    Andrews, B., Carroll, J., Ding, S., Fearnley, I. M. & Walker, J. E. Assembly factors for the membrane arm of human complex I. Proc. Natl Acad. Sci. USA 110, 18934–18939 (2013)

    ADS  CAS  PubMed  Article  Google Scholar 

  28. 28

    Baradaran, R., Berrisford, J. M., Minhas, G. S. & Sazanov, L. A. Crystal structure of the entire respiratory complex I. Nature 494, 443–448 (2013)

    ADS  CAS  PubMed  PubMed Central  Article  Google Scholar 

  29. 29

    Berrisford, J. M. & Sazanov, L. A. Structural basis for the mechanism of respiratory complex I. J. Biol. Chem. 284, 29773–29783 (2009)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  30. 30

    Efremov, R. G., Baradaran, R. & Sazanov, L. A. The architecture of respiratory complex I. Nature 465, 441–445 (2010)

    ADS  CAS  PubMed  Article  Google Scholar 

  31. 31

    Efremov, R. G. & Sazanov, L. A. Structure of the membrane domain of respiratory complex I. Nature 476, 414–420 (2011)

    ADS  CAS  PubMed  Article  Google Scholar 

  32. 32

    Sazanov, L. A. & Hinchliffe, P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430–1436 (2006)

    ADS  CAS  PubMed  Article  Google Scholar 

  33. 33

    Zhang, Z. et al. Electron transfer by domain movement in cytochrome bc1 . Nature 392, 677–684 (1998)

    ADS  CAS  PubMed  Article  Google Scholar 

  34. 34

    Iwata, M., Björkman, J. & Iwata, S. Conformational change of the Rieske [2Fe-2S] protein in cytochrome bc1 complex. J. Bioenerg. Biomembr. 31, 169–175 (1999)

    CAS  PubMed  Article  Google Scholar 

  35. 35

    Berger, I. et al. Mitochondrial complex I deficiency caused by a deleterious NDUFA11 mutation. Ann. Neurol. 63, 405–408 (2008)

    CAS  PubMed  Article  Google Scholar 

  36. 36

    Angerer, H. et al. The LYR protein subunit NB4M/NDUFA6 of mitochondrial complex I anchors an acyl carrier protein and is essential for catalytic activity. Proc. Natl Acad. Sci. USA 111, 5207–5212 (2014)

    ADS  CAS  PubMed  Article  Google Scholar 

  37. 37

    Haack, T. B. et al. Mutation screening of 75 candidate genes in 152 complex I deficiency cases identifies pathogenic variants in 16 genes including NDUFB9. J. Med. Genet. 49, 83–89 (2012)

    CAS  PubMed  Article  Google Scholar 

  38. 38

    Tan, A. S., Baty, J. W. & Berridge, M. V. The role of mitochondrial electron transport in tumorigenesis and metastasis. Biochim. Biophys. Acta 1840, 1454–1463 (2014)

    CAS  PubMed  Article  Google Scholar 

  39. 39

    Ikeda, K., Shiba, S., Horie-Inoue, K., Shimokata, K. & Inoue, S. A stabilizing factor for mitochondrial respiratory supercomplex assembly regulates energy metabolism in muscle. Nature Commun. 4, 2147 (2013)

    ADS  Article  CAS  Google Scholar 

  40. 40

    Williams, E. G. et al. Systems proteomics of liver mitochondria function. Science 352, aad0189 (2016)

    PubMed  Article  CAS  Google Scholar 

  41. 41

    Mourier, A., Matic, S., Ruzzenente, B., Larsson, N. G. & Milenkovic, D. The respiratory chain supercomplex organization is independent of COX7a2l isoforms. Cell Metab. 20, 1069–1075 (2014)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  42. 42

    Lapuente-Brun, E. et al. Supercomplex assembly determines electron flux in the mitochondrial electron transport chain. Science 340, 1567–1570 (2013)

    ADS  CAS  PubMed  Article  Google Scholar 

  43. 43

    Sharpley, M. S., Shannon, R. J., Draghi, F. & Hirst, J. Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria. Biochemistry 45, 241–248 (2006)

    CAS  PubMed  Article  Google Scholar 

  44. 44

    Pfeiffer, K. et al. Cardiolipin stabilizes respiratory chain supercomplexes. J. Biol. Chem. 278, 52873–52880 (2003)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  45. 45

    Radermacher, M. et al. The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme. J. Struct. Biol. 154, 269–279 (2006)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  46. 46

    Hackenbrock, C. R., Chazotte, B. & Gupte, S. S. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J. Bioenerg. Biomembr. 18, 331–368 (1986)

    CAS  PubMed  Article  Google Scholar 

  47. 47

    Chance, B. & Williams, G. R. Respiratory enzymes in oxidative phosphorylation. III. The steady state. J. Biol. Chem. 217, 409–427 (1955)

    CAS  PubMed  Google Scholar 

  48. 48

    Nicastro, D., Frangakis, A. S., Typke, D. & Baumeister, W. Cryo-electron tomography of Neurospora mitochondria. J. Struct. Biol. 129, 48–56 (2000)

    CAS  PubMed  Article  Google Scholar 

  49. 49

    Allen, R. D., Schroeder, C. C. & Fok, A. K. An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J. Cell Biol. 108, 2233–2240 (1989)

    CAS  PubMed  Article  Google Scholar 

  50. 50

    Davies, K. M. et al. Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc. Natl Acad. Sci. USA 108, 14121–14126 (2011)

    ADS  CAS  PubMed  Article  Google Scholar 

  51. 51

    Wittig, I., Braun, H. P. & Schägger, H. Blue native PAGE. Nature Protocols 1, 418–428 (2006)

    CAS  PubMed  Article  Google Scholar 

  52. 52

    Kuonen, D. R., Roberts, P. J. & Cottingham, I. R. Purification and analysis of mitochondrial membrane proteins on nondenaturing gradient polyacrylamide gels. Anal. Biochem. 153, 221–226 (1986)

    CAS  PubMed  Article  Google Scholar 

  53. 53

    Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38–46 (2007)

    CAS  Article  PubMed  PubMed Central  Google Scholar 

  54. 54

    Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  55. 55

    Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods 10, 584–590 (2013)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  56. 56

    Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334–347 (2003)

    PubMed  PubMed Central  Article  Google Scholar 

  57. 57

    Ge, J. et al. Architecture of the mammalian mechanosensitive Piezo1 channel. Nature 527, 64–69 (2015)

    ADS  CAS  Article  Google Scholar 

  58. 58

    Voorhees, R. M., Fernández, I. S., Scheres, S. H. & Hegde, R. S. Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution. Cell 157, 1632–1643 (2014)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  59. 59

    Greber, B. J. et al. The complete structure of the large subunit of the mammalian mitochondrial ribosome. Nature 515, 283–286 (2014)

    ADS  CAS  PubMed  Article  Google Scholar 

  60. 60

    Brown, A. et al. Structure of the large ribosomal subunit from human mitochondria. Science 346, 718–722 (2014)

    ADS  CAS  PubMed  PubMed Central  Article  Google Scholar 

  61. 61

    Fernández, I. S., Bai, X. C., Murshudov, G., Scheres, S. H. & Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823–831 (2014)

    PubMed  PubMed Central  Article  CAS  Google Scholar 

  62. 62

    Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853–854 (2012)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  63. 63

    Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24–35 (2013)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  64. 64

    Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63–65 (2014)

    CAS  Article  Google Scholar 

  65. 65

    Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N. & Sternberg, M. J. The Phyre2 web portal for protein modeling, prediction and analysis. Nature Protocols 10, 845–858 (2015)

    CAS  PubMed  PubMed Central  Article  Google Scholar 

  66. 66

    Pettersen, E. F. et al. UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004). 10.1002/jcc.20084

    CAS  Article  PubMed  PubMed Central  Google Scholar 

  67. 67

    Solmaz, S. R. & Hunte, C. Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J. Biol. Chem. 283, 17542–17549 (2008)

    CAS  PubMed  Article  Google Scholar 

Download references

Acknowledgements

We would like to thank the staff members X. Li, F. Yang and Y. Li of Tsinghua University Branch of China National Center for Protein Sciences (Beijing, China) for providing the facility support. This work was supported by funds from the Ministry of Science and Technology (2016YFA0501101 and 2012CB911101 to M.J., and 2013CB910404 and 2016YFA0500700 to N.G.), and the National Outstanding Young Scholar Science Foundation and National Natural Science Foundation of China (31030020 and 31170679 to M.Y., 31422016 to N.G.).

Author information

Affiliations

Authors

Contributions

M.Y. conceived, designed and supervised the project, analysed data and wrote the manuscript. J.G. and R.G. did the protein purification and detergent screening. M.W. performed electron microscopy sample preparation, data collection and structural determination with help of K.Y., N.G. and J.L. All authors discussed the data and read the manuscript.

Corresponding authors

Correspondence to Ning Gao or Maojun Yang.

Ethics declarations

Competing interests

The authors declare no competing financial interests.

Additional information

Reviewer Information

Nature thanks A. Engel, D. Winge, and the other anonymous reviewer(s) for their contribution to the peer review of this work.

Extended data figures and tables

Extended Data Figure 1 Biochemical characterization of the respiratory supercomplexes.

a, Fractions of sucrose gradient ultracentrifugation were analysed by BNPA. b, In-gel staining of the native gel by NBT. Higher-molecular-weight bands were indicated by a red arrow. c, A representative trace of size-exclusion chromatography of the respiratory supercomplexes. d, Protein samples of the size-exclusion chromatography fractions were subjected to BNPA. Fractions of 9–9.5 ml (elution volume) were used for negative staining EM and cryo-EM. e, NBT staining of the size-exclusion chromatography BNPA.

Extended Data Figure 2 Negative staining EM analysis of the respirasome.

a, A representative micrograph of negatively stained respirasomes. b, 2D class averages of negatively stained particles. c, A flowchart of th einitial model generation and validation. A density ball was used as the initial reference for 3D classification. Results of 3D classification are shown on the right, with class 1, class 2 and class 3 containing 3,031, 2,308 and 4,597 particles, respectively. Bottom left shows the final model used for the 3D refinement of cryo-EM particles.

Extended Data Figure 3 Representative raw cryo-EM particles of the respirasome.

a, A representative cryo-EM micrograph of respirasome. b, Power-spectrum of the micrograph in a. The white circle indicates the 3.0 Å frequency. c, A collection of raw particles of the respirasome collected with Titan Krios (300 kV) and Falcon II. d, Representative 2D class averages in different views.

Extended Data Figure 4 Workflow of 3D classification and refinement of cryo-EM particles.

Workflow of 3D reconstruction with cryo-EM data. A total of 81,100 particles were kept after 2D classification, and subject to two rounds of 3D classification. A final data set containing ~50,000 particles were used for high-resolution refinement (see Methods for more details).

Extended Data Figure 5 Statistics of the final density map of the respirasome.

a, Local resolution map of the final 3D density map. From left to right are respectively side, top and bottom views. b, Gold-standard Fourier shell correlation (FSC) curve of the final density map, after correction of the soft-mask-induced effects. c, Particle orientation distributions in the last iteration of the structural refinement. Red cylinders mean more particles on these orientations. Heights of cylinders represent the relative numbers of particles.

Extended Data Figure 6 Structural assignment of CI and CIII.

a, Gold-standard fourier shell Correlation (FSC) curves of the density maps of CI and CIII obtained by subregion refinement. Both the maps of CI and CIII were refined to a resolution of 3.97 Å. b, The density map (blue meshes) of CI is displayed at root mean squared deviation (r.m.s.d.) = 12 contour level. The backbones of core subunits are shown in the density. c, The density map (blue meshes) of the TM helices of ND2 is displayed at r.m.s.d. = 12 contour level to illustrate the well-resolved side chains of ND2 at a resolution of 3.97 Å after subregion refinement. The residues are shown in line representation and three of them are labelled. The figure was prepared with Coot. d, CIII in our structure of the respirasome is in the intermediate state. The distances between [2Fe-2S] to haem c1, and [2Fe-2S] to haem bL in the final refined CIII structure are 30 Å and 27 Å, respectively. Different subunits are coloured individually as indicated. The figure was generated using PyMOL.

Extended Data Figure 7 Cytochrome c is probably not present in the density map of the respirasome.

The expected positions of cytochrome c are based on the fitting of the structures of CIII with bound cytochrome c from yeast (PDB accession code 3CX5)67. The two cytochrome c molecules of CIII are shown as blue and pink cartoons, respectively. The transmembrane region is indicated by two dashed lines. M, matrix; IM, inner membrane; IMS, intermembrane space.

Extended Data Figure 8 The density map of NDUFA11, NDUFAB1 and NDUFB9.

a, The density map (blue meshes) of NDUFA11 is displayed at r.m.s.d. = 12 contour level. The backbone is shown in line and the N and C termini are indicated. b, The density map (blue meshes) of NDUFAB1 and NDUFB9 is displayed at r.m.s.d. = 12 contour level. The backbones are coloured in orange and yellow, respectively, and the N and C termini are indicated.

Extended Data Figure 9 Sequence alignments of NDUFB9, NDUFA11 and UQCRC1 from different species

. a. Sequence alignment of the NDUFB9 subunit of CI from different species. b, Sequence alignment of the NDUFA11 subunit of CI from different species. c, Sequence alignment of the UQCRC1 binding motif from different species. All alignments were carried out using DNAMAN.

Extended Data Figure 10 Conformational change of CI.

a, Conformational changes of the core and assigned supernumerary subunits of CI. The model of CI in the respirasome (with subunits individually coloured) is globally aligned to the model of free CI (PDB accession code 4UQ8) (coloured in cyan). b, Comparison of the seven matrix core subunits of CI in the free form and in the respirasome. The polypeptides are indicated in different colours and labelled with text in the same colour. c, Same as b, but indicating the comparison of the seven membrane-bound core subunits. The bottom panel is viewed from the matrix side.

PowerPoint slides

Rights and permissions

Reprints and Permissions

About this article

Verify currency and authenticity via CrossMark

Cite this article

Gu, J., Wu, M., Guo, R. et al. The architecture of the mammalian respirasome. Nature 537, 639–643 (2016). https://doi.org/10.1038/nature19359

Download citation

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing