Monomer and dimer structures of cytochrome bo 3 ubiquinol oxidase from Escherichia coli
- Department of Biophysics The University of Texas Southwestern Medical Center Dallas Texas USA, Ligo Analytics Dallas Texas USA
- Department of Microbiology, Immunology and Infectious Diseases University of Calgary Calgary Alberta Canada, Center for Structural Genomics of Infectious Diseases (CSGID) Chicago Illinois USA, Centers for Research on Structural Biology of Infectious Diseases (CSBID) Chicago Illinois USA
- Department of Biophysics The University of Texas Southwestern Medical Center Dallas Texas USA, Center for Structural Genomics of Infectious Diseases (CSGID) Chicago Illinois USA, Centers for Research on Structural Biology of Infectious Diseases (CSBID) Chicago Illinois USA
- Department of Biophysics The University of Texas Southwestern Medical Center Dallas Texas USA, Center for Structural Genomics of Infectious Diseases (CSGID) Chicago Illinois USA, Centers for Research on Structural Biology of Infectious Diseases (CSBID) Chicago Illinois USA, Department of Biochemistry The University of Texas Southwestern Medical Center Dallas Texas USA
- Department of Microbiology, Immunology and Infectious Diseases University of Calgary Calgary Alberta Canada, Center for Structural Genomics of Infectious Diseases (CSGID) Chicago Illinois USA, Centers for Research on Structural Biology of Infectious Diseases (CSBID) Chicago Illinois USA, BioZone, Department of Chemical Engineering and Applied Chemistry University of Toronto Toronto Ontario Canada
Abstract The Escherichia coli cytochrome bo 3 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 3 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).
- Research Organization:
- Ligo Analytics, Dallas, TX (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC); Cancer Prevention and Research Institute of Texas; National Institutes of Health (NIH)
- Grant/Contract Number:
- DE‐SC0019600; DE‐SC0021600; SC0019600; SC0021600; RP170644; RP220582; 75N93022C00035; HHSN272201700060C; R35GM145365
- OSTI ID:
- 1963319
- Alternate ID(s):
- OSTI ID: 1963321; OSTI ID: 1987657
- Journal Information:
- Protein Science, Journal Name: Protein Science Vol. 32 Journal Issue: 4; ISSN 0961-8368
- Publisher:
- Wiley Blackwell (John Wiley & Sons)Copyright Statement
- Country of Publication:
- United Kingdom
- Language:
- English
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