- EMDB-13117: High resolution structure of cytochrome bd-II oxidase from E. col... -
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Database: EMDB / ID: EMD-13117
Title
High resolution structure of cytochrome bd-II oxidase from E. coli at 2.46 A resolution
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Sample
Complex: Cytochrome bd-II oxidase from E. coli composed of subunits AppB, AppC and AppX
Function / homology
Function and homology information
ubiquinol oxidase (H+-transporting) / cytochrome bo3 ubiquinol oxidase activity / cytochrome complex / aerobic electron transport chain / oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor / cell outer membrane / electron transfer activity / heme binding / membrane / metal ion binding / plasma membrane Similarity search - Function
Journal: Proc Natl Acad Sci U S A / Year: 2021 Title: Mechanistic and structural diversity between cytochrome isoforms of . Authors: Tamara N Grund / Melanie Radloff / Di Wu / Hojjat G Goojani / Luca F Witte / Wiebke Jösting / Sabine Buschmann / Hannelore Müller / Isam Elamri / Sonja Welsch / Harald Schwalbe / Hartmut ...Authors: Tamara N Grund / Melanie Radloff / Di Wu / Hojjat G Goojani / Luca F Witte / Wiebke Jösting / Sabine Buschmann / Hannelore Müller / Isam Elamri / Sonja Welsch / Harald Schwalbe / Hartmut Michel / Dirk Bald / Schara Safarian / Abstract: The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome -type oxygen reductase is ...The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome -type oxygen reductase is a critical survival factor utilized by pathogenic bacteria during infection, proliferation and the transition from acute to chronic states. encodes for two cytochrome isoforms that are both involved in respiration under oxygen limited conditions. Mechanistic and structural differences between () and () operon encoded cytochrome variants have remained elusive in the past. Here, we demonstrate that cytochrome - catalyzes oxidation of benzoquinols while possessing additional specificity for naphthoquinones. Our data show that although menaquinol-1 (MK1) is not able to directly transfer electrons onto cytochrome from , it has a stimulatory effect on its oxygen reduction rate in the presence of ubiquinol-1. We further determined cryo-EM structures of cytochrome - to high resolution of 2.1 Å. Our structural insights confirm that the general architecture and substrate accessible pathways are conserved between the two oxidase isoforms, but two notable differences are apparent upon inspection: (i) does not contain a CydH-like subunit, thereby exposing heme to the membrane environment and (ii) the AppB subunit harbors a structural demethylmenaquinone-8 molecule instead of ubiquinone-8 as found in CydB of Our work completes the structural landscape of terminal respiratory oxygen reductases of and suggests that structural and functional properties of the respective oxidases are linked to quinol-pool dependent metabolic adaptations in .
History
Deposition
Jun 24, 2021
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Header (metadata) release
Dec 15, 2021
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Map release
Dec 15, 2021
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Update
Dec 15, 2021
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Current status
Dec 15, 2021
Processing site: PDBe / Status: Released
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Surface view with section colored by density value
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