Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 Å resolution.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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OriginalspracheEnglisch
Seiten (von - bis)142-156
Seitenumfang15
FachzeitschriftNature plants
Jahrgang9
Ausgabenummer1
Frühes Online-Datum30 Dez. 2022
PublikationsstatusVeröffentlicht - Jan. 2023

Abstract

Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III 2 with a co-purified ubiquinone in the Q O site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.

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Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 Å resolution. / Klusch, Niklas; Dreimann, Maximilian; Senkler, Jennifer et al.
in: Nature plants, Jahrgang 9, Nr. 1, 01.2023, S. 142-156.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

Klusch N, Dreimann M, Senkler J, Rugen N, Kühlbrandt W, Braun HP. Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 Å resolution. Nature plants. 2023 Jan;9(1):142-156. Epub 2022 Dez 30. doi: 10.1038/s41477-022-01308-6
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title = "Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 {\AA} resolution.",
abstract = "Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III 2 with a co-purified ubiquinone in the Q O site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane. ",
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AU - Klusch, Niklas

AU - Dreimann, Maximilian

AU - Senkler, Jennifer

AU - Rugen, Nils

AU - Kühlbrandt, Werner

AU - Braun, Hans-Peter

N1 - Funding Information: We thank Ö. Yildiz for help in building the atomic model and interpreting the cryo-EM structure. This work was funded by the Max Planck Society (W.K., M.D. and N.K.) and by the Deutsche Forschungsgemeinschaft (grant INST 187/791-1 FUGG to H.-P.B.; SFB 807 to W.K. and N.K.).

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N2 - Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III 2 with a co-purified ubiquinone in the Q O site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.

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