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Active site rearrangement and structural divergence in prokaryotic respiratory oxidases
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Active site rearrangement and structural divergence in prokaryotic respiratory oxidases
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Journal Article
Active site rearrangement and structural divergence in prokaryotic respiratory oxidases
2019
Overview
Cytochrome bd–type quinol oxidases catalyze the reduction of molecular oxygen to water in the respiratory chain of many human-pathogenic bacteria. They are structurally unrelated to mitochondrial cytochrome c oxidases and are therefore a prime target for the development of antimicrobial drugs. We determined the structure of the Escherichia coli cytochrome bd-I oxidase by single-particle cryo–electron microscopy to a resolution of 2.7 angstroms. Our structure contains a previously unknown accessory subunit CydH, the L-subfamily–specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an oxygen-conducting pathway. Comparison with another cytochrome bd oxidase reveals structural divergence in the family, including rearrangement of high-spin hemes and conformational adaption of a transmembrane helix to generate a distinct oxygen-binding site.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science,American Association for the Advancement of Science (AAAS)
Subject
Antiinfectives and antibacterials
/ Bacteria
/ Biochemistry, Molecular Biology
/ Channels
/ Cytochrome b Group - chemistry
/ E coli
/ Electron Transport Chain Complex Proteins - chemistry
/ Enzymes
/ Escherichia coli - enzymology
/ Escherichia coli Proteins - chemistry
/ Heme
/ Homology
/ Oxidase
/ Oxygen
/ Protein Structure, Quaternary
/ Protein Subunits - chemistry
/ Protons
/ Structure-function relationships
/ Water
