Climate Change Data Portal
DOI | 10.1073/pnas.2114013118 |
Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli | |
Grund T.N.; Radloff M.; Wu D.; Goojani H.G.; Witte L.F.; Jösting W.; Buschmann S.; Müller H.; Elamri I.; Welsch S.; Schwalbe H.; Michel H.; Bald D.; Safarian S. | |
发表日期 | 2021 |
ISSN | 0027-8424 |
卷号 | 118期号:50 |
英文摘要 | The treatment of infectious diseases caused by multidrug-resistant pathogens is a major clinical challenge of the 21st century. The membrane-embedded respiratory cytochrome bd-type oxygen reductase is a critical survival factor utilized by pathogenic bacteria during infection, proliferation and the transition from acute to chronic states. Escherichia coli encodes for two cytochrome bd isoforms that are both involved in respiration under oxygen limited conditions. Mechanistic and structural differences between cydABX (Ecbd-I) and appCBX (Ecbd-II) operon encoded cytochrome bd variants have remained elusive in the past. Here, we demonstrate that cytochrome bd-II 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 bd-II from E. coli, it has a stimulatory effect on its oxygen reduction rate in the presence of ubiquinol-1. We further determined cryo-EM structures of cytochrome bd-II to high resolution of 2.1 Å. Our structural insights confirm that the general architecture and substrate accessible pathways are conserved between the two bd oxidase isoforms, but two notable differences are apparent upon inspection: (i) Ecbd-II does not contain a CydH-like subunit, thereby exposing heme b595 to the membrane environment and (ii) the AppB subunit harbors a structural demethylmenaquinone-8 molecule instead of ubiquinone-8 as found in CydB of Ecbd-I. Our work completes the structural landscape of terminal respiratory oxygen reductases of E. coli and suggests that structural and functional properties of the respective oxidases are linked to quinol-pool dependent metabolic adaptations in E. coli. © 2021 National Academy of Sciences. All rights reserved. |
英文关键词 | AppC; Bd oxidase; Microbiology; Respiration; Structural biology |
语种 | 英语 |
scopus关键词 | cytochrome; cytochrome bd; heme; hydroquinone; isoenzyme; menaquinol 1; naphthoquinone; oxidoreductase; oxygen; quinone derivative; ubiquinol; ubiquinol 1; ubiquinone; unclassified drug; cytochrome b; cytochrome bd terminal oxidase complex, E coli; Escherichia coli protein; isoprotein; multienzyme complex; oxidoreductase; Article; catalysis; cryoelectron microscopy; electron transport; enzyme mechanism; enzyme specificity; enzyme structure; enzyme substrate; enzyme subunit; Escherichia coli; microbial diversity; microbial respiration; microbiology; nonhuman; operon; oxidation; structure analysis; Escherichia coli; gene expression regulation; genetics; metabolism; molecular model; physiology; protein conformation; Cytochrome b Group; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Models, Molecular; Oxidoreductases; Protein Conformation; Protein Isoforms |
来源期刊 | Proceedings of the National Academy of Sciences of the United States of America |
文献类型 | 期刊论文 |
条目标识符 | http://gcip.llas.ac.cn/handle/2XKMVOVA/250933 |
作者单位 | Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, D-60438, Germany; Department of Molecular Cell Biology, Amsterdam Institute of Molecular and Life Sciences, Faculty of Science, Vrije Universiteit Amsterdam, Amsterdam, 1081 HZ, Netherlands; Center for Biomolecular Magnetic Resonance, Institute of Organic Chemistry and Chemical Biology, Goethe Universität Frankfurt am Main, Frankfurt am Main, 60438, Germany; Central Electron Microscopy Facility, Max Planck Institute of Biophysics, Frankfurt am Main, D-60438, Germany |
推荐引用方式 GB/T 7714 | Grund T.N.,Radloff M.,Wu D.,et al. Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli[J],2021,118(50). |
APA | Grund T.N..,Radloff M..,Wu D..,Goojani H.G..,Witte L.F..,...&Safarian S..(2021).Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America,118(50). |
MLA | Grund T.N.,et al."Mechanistic and structural diversity between cytochrome bd isoforms of Escherichia coli".Proceedings of the National Academy of Sciences of the United States of America 118.50(2021). |
条目包含的文件 | 条目无相关文件。 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。