8aba | pdb_00008aba

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

spinqualitylabelsall models 8aba, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8aba is a 20 chain structure with sequence from Yarrowia lipolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.2Å Ligands: CDL, FES, HEC, HEM, LMT, PC1, PTY, XP4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CYB_YARLI Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.[UniProtKB:P00163] Publication Abstract from PubMed Movement of the Rieske domain of the iron-sulfur protein is essential for intramolecular electron transfer within complex III(2) (CIII(2)) 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(2) from Yarrowia lipolytica at resolutions up to 2.0 A 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(2) with a reduced high-potential chain increased the occupancy of the Q(o) site. The extent of Rieske domain interactions through hydrogen bonds to the cytochrome b and cytochrome c(1) 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(1) than in the oxidized state. Upon addition of the inhibitor antimycin A, the heterogeneity of the cd(1)-helix and ef-loop increased, which may be indicative of a long-range effect on the Rieske domain. Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III(2) by cryo-EM.,Wieferig JP, Kuhlbrandt W IUCrJ. 2023 Jan 1;10(Pt 1):27-37. doi: 10.1107/S2052252522010570. PMID:36598500 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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