ArticleBiochemistry2013
Structural organization of FtsB, a transmembrane protein of the bacterial divisome.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.Biophysical journal · 2025Article
- High-throughput discovery of transmembrane helix dimers from human single-pass membrane proteins with TOXGREEN sort-seq.PNAS nexus · 2025Article
- 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
- GLTM: A Global-Local Attention LSTM Model to Locate Dimer Motif of Single-Pass Membrane Proteins.Frontiers in genetics · 2022Article
- 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
- Article
- Experimental determination and data-driven prediction of homotypic transmembrane domain interfaces.Computational and structural biotechnology journal · 2020Article
- Lipid Binding Controls Dimerization of the Coat Protein p24 Transmembrane Helix.Biophysical journal · 2019Article
- Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome.Scientific reports · 2018Article
- Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB.mBio · 2018Article
- The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions.The Journal of biological chemistry · 2018Article
- Combination of Cα-H Hydrogen Bonds and van der Waals Packing Modulates the Stability of GxxxG-Mediated Dimers in Membranes.Journal of the American Chemical Society · 2017Article
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes.The EMBO journal · 2016Article
- The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.The Journal of biological chemistry · 2015Article
- Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET.Biopolymers · 2015Review
- Roles for both FtsA and the FtsBLQ subcomplex in FtsN-stimulated cell constriction in Escherichia coli.Molecular microbiology · 2015Article
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Authors and funding
6 authors.
Funding
Abstract
We report the first structural analysis of an integral membrane protein of the bacterial divisome. FtsB is a single-pass membrane protein with a periplasmic coiled coil. Its heterologous association with its partner FtsL represents an essential event for the recruitment of the late components to the division site. Using a combination of mutagenesis, computational modeling, and X-ray crystallography, we determined that FtsB self-associates, and we investigated its structural organization. We found that the transmembrane domain of FtsB homo-oligomerizes through an evolutionarily conserved interaction interface where a polar residue (Gln 16) plays a critical role through the formation of an interhelical hydrogen bond. The crystal structure of the periplasmic domain, solved as a fusion with Gp7, shows that 30 juxta-membrane amino acids of FtsB form a canonical coiled coil. The presence of conserved Gly residue in the linker region suggests that flexibility between the transmembrane and coiled coil domains is functionally important. We hypothesize that the transmembrane helices of FtsB form a stable dimeric core for its association with FtsL into a higher-order oligomer and that FtsL is required to stabilize the periplasmic domain of FtsB, leading to the formation of a complex that is competent for binding to FtsQ, and to their consequent recruitment to the divisome. The study provides an experimentally validated structural model and identifies point mutations that disrupt association, thereby establishing important groundwork for the functional characterization of FtsB in vivo.
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