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-Structure paper
Title | Atomic structures of respiratory complex III, complex IV, and supercomplex III-IV from vascular plants. |
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Journal, issue, pages | Elife, Vol. 10, Year 2021 |
Publish date | Jan 19, 2021 |
![]() | Maria Maldonado / Fei Guo / James A Letts / ![]() |
PubMed Abstract | Mitochondrial complex III (CIII) and complex IV (CIV), which can associate into a higher-order supercomplex (SC III+IV), play key roles in respiration. However, structures of these plant complexes ...Mitochondrial complex III (CIII) and complex IV (CIV), which can associate into a higher-order supercomplex (SC III+IV), play key roles in respiration. However, structures of these plant complexes remain unknown. We present atomic models of CIII, CIV, and SC III+IV from determined by single-particle cryoEM. The structures reveal plant-specific differences in the MPP domain of CIII and define the subunit composition of CIV. Conformational heterogeneity analysis of CIII revealed long-range, coordinated movements across the complex, as well as the motion of CIII'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. |
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Methods | EM (single particle) |
Resolution | 3.2 - 3.8 Å |
Structure data | EMDB-22445, PDB-7jrg: EMDB-22447, PDB-7jro: EMDB-22448: Plant Mitochondrial complex SC III2+IV from Vigna radiata composite map ![]() EMDB-22449: ![]() EMDB-22450: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-PC1: ![]() ChemComp-CDL: ![]() ChemComp-HEM: ![]() ChemComp-3PE: ![]() ChemComp-HEC: ![]() ChemComp-HEA: ![]() ChemComp-CU: ![]() ChemComp-MG: ![]() ChemComp-CUA: ![]() ChemComp-LYS: |
Source |
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![]() | ELECTRON TRANSPORT / mitochondria / respiration / bioenergetics / plants / OXIDOREDUCTASE |