ArticleNature communications2020
Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Adaptations in electron transport chain complexes of clinical Rhodococcus equi revealed through comparative genomics.World journal of microbiology & biotechnology · 2026Article
- Sesamol derivatives bearing a quinazolin moiety: synthesis, antifungal efficacy against tea plant pathogens, and mechanistic insights.Natural products and bioprospecting · 2026Article
- Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026Article
- Cryo-EM structure of bixafen-bound S. cerevisiae complex II unravels SDHI specificity against pathogenic fungi.Communications biology · 2026Article
- Inactivation of cAMP receptor protein (MSMEG_6189) increases isoniazid susceptibility inJournal of bacteriology · 2025Article
- Structural basis of menaquinone reduction by succinate dehydrogenase from Chloroflexus aurantiacus.Nature communications · 2025Article
- Remission spectroscopy resolves the mechanism of action of bedaquiline within living mycobacteria.Nature communications · 2025Article
- Cryo-EM structure of the yeast Saccharomyces cerevisiae SDH provides a template for eco-friendly fungicide discovery.Nature communications · 2025Article
- TCMD: A High-Throughput and Rapid Method for Screening Antimicrobial Ingredients from Renewable Bio-Based Resources.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Cryo-EM of native membranes reveals an intimate connection between the Krebs cycle and aerobic respiration in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the Chemical Space of Mycobacterial Oxidative Phosphorylation Inhibitors Using Molecular Modeling.ChemMedChem · 2024Review
- Copper Resistance Mechanism and Copper Response Genes inMicroorganisms · 2024Article
- Cryo-EM structures of a prokaryotic heme transporter CydDC.Protein & cell · 2023Article
- Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023Article
- An evolving view of complex II-noncanonical complexes, megacomplexes, respiration, signaling, and beyond.The Journal of biological chemistry · 2023Review
- Structure of the human respiratory complex II.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure of mycobacterial respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Uncovering interactions between mycobacterial respiratory complexes to target drug-resistantFrontiers in cellular and infection microbiology · 2022Review
- Crystallographic investigation of the ubiquinone binding site of respiratory Complex II and its inhibitors.Biochimica et biophysica acta. Proteins and proteomics · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
17 authors at 8 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria but little is known about the catalytic mechanisms they employ for succinate oxidation by menaquinone. Here, we present the 2.8 Å cryo-electron microscopy structure of a Mycobacterium smegmatis Sdh, which forms a trimer. We identified the membrane-anchored SdhF as a subunit of the complex. The 3 kDa SdhF forms a single transmembrane helix and this helix plays a role in blocking the canonically proximal quinone-binding site. We also identified two distal quinone-binding sites with bound quinones. One distal binding site is formed by neighboring subunits of the complex. Our structure further reveals the electron/proton transfer pathway for succinate oxidation by menaquinone. Moreover, this study provides further structural insights into the physiological significance of a trimeric respiratory complex II. The structure of the menaquinone binding site could provide a framework for the development of Sdh-selective anti-mycobacterial drugs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.