ArticleScientific reports2018
Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- FtsW protein-protein interactions visualized in live Staphylococcus aureus cells by FLIM-FRET.Nature communications · 2026Article
- In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026Article
- FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Postbiotics in the Bakery Products: Applications and Nutritional Values.Probiotics and antimicrobial proteins · 2025Review
- Article
- Insights into the assembly and regulation of the bacterial divisome.Nature reviews. Microbiology · 2024Review
- The Impact of COVID-19 on HIV Care in Rio de Janeiro, Brazil 2019-2021: Disparities by Age and Gender.AIDS and behavior · 2023Article
- Conformational changes in the essential E. coli septal cell wall synthesis complex suggest an activation mechanism.Nature communications · 2023Article
- Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL.Nature microbiology · 2023Article
- Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome.Nature communications · 2023Article
- The structural integrity of the membrane-embedded bacterial division complex FtsQBL studied with molecular dynamics simulations.Computational and structural biotechnology journal · 2023Article
- Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.Journal of the American Chemical Society · 2022Article
- Filamentous Thermosensitive Mutant Z: An Appealing Target for Emerging Pathogens and a Trek on Its Natural Inhibitors.Biology · 2022Review
- An Updated Model of the Divisome: Regulation of the Septal Peptidoglycan Synthesis Machinery by the Divisome.International journal of molecular sciences · 2022Review
- Mapping the FtsQBL divisome components in bacterial NTD pathogens as potential drug targets.Frontiers in genetics · 2022Article
- The coiled-coil domain of Escherichia coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division.The Journal of biological chemistry · 2022Article
- FtsA acts through FtsW to promote cell wall synthesis during cell division inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Predictive approaches to guide the expression of recombinant vaccine targets in Escherichia coli: a case study presentation utilising Absynth Biologics Ltd. proprietary Clostridium difficile vaccine antigens.Applied microbiology and biotechnology · 2021Article
- A Comprehensive Evolutionary Scenario of Cell Division and Associated Processes in the Firmicutes.Molecular biology and evolution · 2021Article
- Integrated Proteomic and Transcriptomic Analyses Reveal the Roles ofFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Bacterial cell division is a fundamental process that results in the physical separation of a mother cell into two daughter cells and involves a set of proteins known as the divisome. Among them, the FtsQ/FtsB/FtsL complex was known as a scaffold protein complex, but its overall structure and exact function is not precisely known. In this study, we have determined the crystal structure of the periplasmic domain of FtsQ in complex with the C-terminal fragment of FtsB, and showed that the C-terminal region of FtsB is a key binding region of FtsQ via mutational analysis in vitro and in vivo. We also obtained the solution structure of the periplasmic FtsQ/FtsB/FtsL complex by small angle X-ray scattering (SAXS), which reveals its structural organization. Interestingly, the SAXS and analytical gel filtration data showed that the FtsQ/FtsB/FtsL complex forms a 2:2:2 heterohexameric assembly in solution with the "Y" shape. Based on the model, the N-terminal directions of FtsQ and the FtsB/FtsL complex should be opposite, suggesting that the Y-shaped FtsQ/FtsB/FtsL complex might fit well into the curved membrane for membrane anchoring.
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