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8ABA

Complex III2 from Yarrowia lipolytica, ascorbate-reduced, int-position

Summary for 8ABA
Entry DOI10.2210/pdb8aba/pdb
EMDB information15316
DescriptorCytochrome b, YALI0C12210p, PROTOPORPHYRIN IX CONTAINING FE, ... (18 entities in total)
Functional Keywordsoxidoreductase, electron transport chain, membrane protein
Biological sourceYarrowia lipolytica
More
Total number of polymer chains20
Total formula weight547055.63
Authors
Wieferig, J.P.,Kuhlbrandt, W. (deposition date: 2022-07-04, release date: 2023-01-11, Last modification date: 2023-01-25)
Primary citationWieferig, J.P.,Kuhlbrandt, W.
Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III 2 by cryo-EM.
Iucrj, 10:27-37, 2023
Cited by
PubMed Abstract: Movement of the Rieske domain of the iron-sulfur protein is essential for intramolecular electron transfer within complex III (CIII) of the respiratory chain as it bridges a gap in the cofactor chain towards the electron acceptor cytochrome c. We present cryo-EM structures of CIII from Yarrowia lipolytica at resolutions up to 2.0 Å under different conditions, with different redox states of the cofactors of the high-potential chain. All possible permutations of three primary positions were observed, indicating that the two halves of the dimeric complex act independently. Addition of the substrate analogue decylubiquinone to CIII with a reduced high-potential chain increased the occupancy of the Q site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c subunits varied depending on the redox state and substrate. In the absence of quinols, the reduced Rieske domain interacted more closely with cytochrome b and cytochrome c than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain.
PubMed: 36598500
DOI: 10.1107/S2052252522010570
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

226707

数据于2024-10-30公开中

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