Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 142-156 |
| Seitenumfang | 15 |
| Fachzeitschrift | Nature plants |
| Jahrgang | 9 |
| Ausgabenummer | 1 |
| Frühes Online-Datum | 30 Dez. 2022 |
| Publikationsstatus | Veröffentlicht - 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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in: Nature plants, Jahrgang 9, Nr. 1, 01.2023, S. 142-156.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 Å resolution.
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.).
PY - 2023/1
Y1 - 2023/1
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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85145194310&partnerID=8YFLogxK
U2 - 10.1038/s41477-022-01308-6
DO - 10.1038/s41477-022-01308-6
M3 - Article
C2 - 36585502
VL - 9
SP - 142
EP - 156
JO - Nature plants
JF - Nature plants
SN - 2055-0278
IS - 1
ER -