8F6C

E. coli cytochrome bo3 ubiquinol oxidase dimer

Summary for 8F6C

• Entry DOI: 10.2210/pdb8f6c/pdb
• EMDB information: 28877 28879
• Descriptor: Cytochrome bo(3) ubiquinol oxidase subunit 1, Cytochrome bo(3) ubiquinol oxidase subunit 2, Cytochrome bo(3) ubiquinol oxidase subunit 3, ... (8 entities in total)
• Functional Keywords: heme-copper oxidase, proton translocation, e. coli aerobic respiratory chain, membrane protein, proton transport
• Biological source: Escherichia coli; More
• Total number of polymer chains: 8
• Total formula weight: 275411.19

Authors

Guo, Y.,Karimullina, E.,Borek, D.,Savchenko, A. (deposition date: 2022-11-16, release date: 2022-11-30, Last modification date: 2024-05-22)

Primary citation

Guo, Y.,Karimullina, E.,Emde, T.,Otwinowski, Z.,Borek, D.,Savchenko, A.
Monomer and dimer structures of cytochrome bo 3 ubiquinol oxidase from Escherichia coli.
Protein Sci., 32:e4616-e4616, 2023

PubMed Abstract: The Escherichia coli cytochrome bo ubiquinol oxidase is a four-subunit heme-copper oxidase that serves as a proton pump in the E. coli aerobic respiratory chain. Despite many mechanistic studies, it is unclear whether this ubiquinol oxidase functions as a monomer, or as a dimer in a manner similar to its eukaryotic counterparts-the mitochondrial electron transport complexes. In this study, we determined the monomeric and dimeric structures of the E. coli cytochrome bo ubiquinol oxidase reconstituted in amphipol by cryogenic electron microscopy single particle reconstruction (cryo-EM SPR) to a resolution of 3.15 and 3.46 Å, respectively. We have discovered that the protein can form a dimer with C2 symmetry, with the dimerization interface maintained by interactions between the subunit II of one monomer and the subunit IV of the other monomer. Moreover, the dimerization does not induce significant structural changes in the monomers, except the movement of a loop in subunit IV (residues 67-74).

PubMed: 36880269
DOI: 10.1002/pro.4616

Experimental method

ELECTRON MICROSCOPY (3.46 Å)