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Atomic structures of respiratory complex III2, complex IV, and supercomplex III2-IV from vascular plants.


ABSTRACT: Mitochondrial complex III (CIII2) and complex IV (CIV), which can associate into a higher-order supercomplex (SC III2+IV), play key roles in respiration. However, structures of these plant complexes remain unknown. We present atomic models of CIII2, CIV, and SC III2+IV from Vigna radiata determined by single-particle cryoEM. The structures reveal plant-specific differences in the MPP domain of CIII2 and define the subunit composition of CIV. Conformational heterogeneity analysis of CIII2 revealed long-range, coordinated movements across the complex, as well as the motion of CIII2's iron-sulfur head domain. The CIV structure suggests that, in plants, proton translocation does not occur via the H channel. The supercomplex interface differs significantly from that in yeast and bacteria in its interacting subunits, angle of approach and limited interactions in the mitochondrial matrix. These structures challenge long-standing assumptions about the plant complexes and generate new mechanistic hypotheses.

SUBMITTER: Maldonado M 

PROVIDER: S-EPMC7815315 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature

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Atomic structures of respiratory complex III<sub>2</sub>, complex IV, and supercomplex III<sub>2</sub>-IV from vascular plants.

Maldonado Maria M   Guo Fei F   Letts James A JA  

eLife 20210119


Mitochondrial complex III (CIII<sub>2</sub>) and complex IV (CIV), which can associate into a higher-order supercomplex (SC III<sub>2</sub>+IV), play key roles in respiration. However, structures of these plant complexes remain unknown. We present atomic models of CIII<sub>2</sub>, CIV, and SC III<sub>2</sub>+IV from <i>Vigna radiata</i> determined by single-particle cryoEM. The structures reveal plant-specific differences in the MPP domain of CIII<sub>2</sub> and define the subunit composition  ...[more]

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