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Title: Monomer and dimer structures of cytochrome bo 3 ubiquinol oxidase from Escherichia coli

Journal Article · · Protein Science
DOI:https://doi.org/10.1002/pro.4616· OSTI ID:1963319
 [1];  [2];  [3];  [4]; ORCiD logo [4]; ORCiD logo [5]
  1. Department of Biophysics The University of Texas Southwestern Medical Center Dallas Texas USA, Ligo Analytics Dallas Texas USA
  2. 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
  3. 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
  4. 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
  5. 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

References (36)

Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding journal June 2016
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 A journal May 1996
Detection of Protein Assemblies in Crystals book January 2005
Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction journal November 2020
Cryo-EM structures of Escherichia coli cytochrome bo 3 reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site journal August 2021
MolProbity : all-atom structure validation for macromolecular crystallography journal December 2009
Cryo-EM single-particle structure refinement and map calculation usingServalcat journal September 2021
Coot model-building tools for molecular graphics journal November 2004
Features and development of Coot journal March 2010
A ‘Build and Retrieve’ methodology to simultaneously solve cryo-EM structures of membrane proteins journal January 2021
REFMAC 5 for the refinement of macromolecular crystal structures journal March 2011
Cytochrome o ( bo ) is a proton pump in Paracoccus denitrificans and Escherichia coli journal June 1989
Artificial intelligence advances for de novo molecular structure modeling in cryo‐electron microscopy journal May 2021
Structural basis of functions of the mitochondrial cytochrome bc1 complex journal June 1998
Triton-X-100 induced dissociation of beef heart cytochrome c oxidase into monomers journal May 1986
The 1.3-Å resolution structure of bovine cytochrome c oxidase suggests a dimerization mechanism journal January 2021
Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix journal October 2019
Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT journal November 2021
Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs journal October 2019
Recent developments in the CCP-EM software suite journal May 2017
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions journal November 2004
Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule. journal February 1996
Electron transfer by domain movement in cytochrome bc1 journal April 1998
Cryo-EM and artificial intelligence visualize endogenous protein community members journal April 2022
Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions journal January 2015
Evidence for dimer structure of proton-pumping cytochrome c oxidase, an analysis by radiation inactivation. journal July 1986
Homologous bd oxidases share the same architecture but differ in mechanism journal November 2019
MOLREP an Automated Program for Molecular Replacement journal December 1997
Real-space refinement in PHENIX for cryo-EM and crystallography journal May 2018
Detergent-solubilized Escherichia coli cytochrome bo 3 ubiquinol oxidase: a monomeric, not a dimeric complex journal August 1999
Inference of Macromolecular Assemblies from Crystalline State journal September 2007
Automated electron microscope tomography using robust prediction of specimen movements journal October 2005
UCSF Chimera?A visualization system for exploratory research and analysis journal January 2004
Assembly of the Cytochrome bo3 Complex journal August 2007
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination journal February 2017
Collaborative Computational Project for Electron cryo-Microscopy journal January 2015

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