ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of the cell wall anchor domain of MotB, a stator component of the bacterial flagellar motor: implications for peptidoglycan recognition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 155 citations in OpenAlex.
- Near-atomic in situ architecture and membrane-coupled dynamics of the Vibrio cholerae sheathed flagellum.Nature communications · 2026Article
- Structural insights into the assembly and evolution of a complex bacterial flagellar motor.Nature microbiology · 2026Article
- Crystal structures of Campylobacter jejuni CadF reveal a potential role for the arginine residue R268 in peptidoglycan recognition and pocket formation.Scientific reports · 2025Article
- Long-range coupling regulates stator dynamics in the bacterial flagellar motor.bioRxiv : the preprint server for biology · 2025Article
- An inner membrane protein is covalently attached to peptidoglycan in the γ-proteobacterium Dickeya dadantii.Communications biology · 2025Article
- Article
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Evolution of a large periplasmic disk in Campylobacterota flagella enables both efficient motility and autoagglutination.Developmental cell · 2024Article
- Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- FliL and its paralog MotF have distinct roles in the stator activity of the Sinorhizobium meliloti flagellar motor.Molecular microbiology · 2022Article
- Heterogeneous glycosylation and methylation of the Aeromonas caviae flagellin.MicrobiologyOpen · 2022Article
- Article
- A physical mechanism underlying the torque generation of the bacterial flagellar motor.The European physical journal. E, Soft matter · 2022Article
- The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacterial Proprioception: Can a Bacterium Sense Its Movement?Frontiers in microbiology · 2022Review
- Modeling Bacterial Flagellar Motor With New Structure Information: Rotational Dynamics of Two Interacting Protein Nano-Rings.Frontiers in microbiology · 2022Article
- The Periplasmic Domain of the Ion-Conducting Stator of Bacterial Flagella Regulates Force Generation.Frontiers in microbiology · 2022Review
- The Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- Force-Generation by the Trans-Envelope Tol-Pal System.Frontiers in microbiology · 2022Review
12 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 2 countries.
Funding
Abstract
The stator ring of the bacterial flagellar motor is composed of the MotA and MotB proteins that act together to generate a turning force (torque) acting on the FliG ring of the rotor. The C-terminal domain of MotB (MotB-C) is believed to anchor the MotA/MotB complex to peptidoglycan (PG) of the cell wall. The first crystal structures of MotB-C and its complex with N-acetylmuramic acid (NAM) have been determined to 1.6- and 2.3-A resolution, respectively. MotB-C is a dimer, both in solution and in the crystal. The two glycan chains of the PG ligand can be modeled as semirigid helices and docked into the grooves harboring the NAM molecules on the opposite faces of the dimer. The model suggests that a concave hydrophilic surface created upon edge-to-edge beta-sheet dimerization and centered around the 2-fold axis of the dimer can accommodate the peptide cross-bridge linking the two sugar chains. Significant structural similarities were found between MotB-C and the PG-binding domains of reduction-modifiable protein M and peptidoglycan-associated lipoprotein exclude, suggesting that PG recognition by different outer membrane protein A-like proteins may be governed by very similar molecular mechanisms that evidently involve protein dimerization.
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