Cryo-EM structure of mycobacterial cytochrome bd reveals two oxygen access channels
| Autor: | Yuezheng Lai, Luke W. Guddat, Quan Wang, Shan Zhou, Yuying Zhang, Fengjiang Liu, Yanting Tang, Yan Gao, Hongri Gong, Zihe Rao, Xiaoting Zhou, Weiwei Wang, Xiuna Yang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Cytochrome Protein Conformation Science Mycobacterium smegmatis Respiratory chain General Physics and Astronomy Heme medicine.disease_cause environment and public health Article General Biochemistry Genetics and Molecular Biology Substrate Specificity Electron Transport 03 medical and health sciences Bacterial Proteins medicine Escherichia coli 030304 developmental biology 0303 health sciences Oxidase test Multidisciplinary biology Chemistry Cryoelectron Microscopy 030302 biochemistry & molecular biology Rational design General Chemistry Cytochrome b Group biology.organism_classification Recombinant Proteins Oxygen Protein Subunits Electron Transport Chain Complex Proteins Biochemistry biology.protein Oxidoreductases Function (biology) Bacteria |
| Zdroj: | Nature Communications, Vol 12, Iss 1, Pp 1-8 (2021) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | Cytochromes bd are ubiquitous amongst prokaryotes including many human-pathogenic bacteria. Such complexes are targets for the development of antimicrobial drugs. However, an understanding of the relationship between the structure and functional mechanisms of these oxidases is incomplete. Here, we have determined the 2.8 Å structure of Mycobacterium smegmatis cytochrome bd by single-particle cryo-electron microscopy. This bd oxidase consists of two subunits CydA and CydB, that adopt a pseudo two-fold symmetrical arrangement. The structural topology of its Q-loop domain, whose function is to bind the substrate, quinol, is significantly different compared to the C-terminal region reported for cytochromes bd from Geobacillus thermodenitrificans (G. th) and Escherichia coli (E. coli). In addition, we have identified two potential oxygen access channels in the structure and shown that similar tunnels also exist in G. th and E. coli cytochromes bd. This study provides insights to develop a framework for the rational design of antituberculosis compounds that block the oxygen access channels of this oxidase. Cytochromes bd oxidase (Cyt-bd) catalyzes the reduction of oxygen to water and is the terminal oxidase in the respiratory chain of prokaryotes. Here, the authors present the 2.8 Å cryo-EM structure of Mycobacterium smegmatis Cyt-bd and identify two potential oxygen access channels in the structure, which is of interest for the development of novel antituberculosis drugs. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink