ArticleScientific reports2016
Structural insights into bacterial flagellar hooks similarities and specificities.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Inhibitors of Lysinoalanine Cross-Linking in the Flagella Hook as Antimicrobials against Spirochetes.ACS chemical biology · 2025Article
- An overview of the structure and function of the flagellar hook FlgE protein.World journal of microbiology & biotechnology · 2023Review
- Dynamic stiffening of the flagellar hook.Nature communications · 2022Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Structure and chemistry of lysinoalanine crosslinking in the spirochaete flagella hook.Nature chemical biology · 2019Article
- Crystal structure of FlgL and its implications for flagellar assembly.Scientific reports · 2018Article
- Structure of FlgK reveals the divergence of the bacterial Hook-Filament Junction of Campylobacter.Scientific reports · 2017Article
- An intrinsically disordered linker controlling the formation and the stability of the bacterial flagellar hook.BMC biology · 2017Article
- Complete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions.Nature communications · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Across bacteria, the protein that makes the flagellar hook, FlgE, has a high variability in amino acid residue composition and sequence length. We hereby present the structure of two fragments of FlgE protein from Campylobacter jejuni and from Caulobacter crescentus, which were obtained by X-ray crystallography, and a high-resolution model of the hook from Caulobacter. By comparing these new structures of FlgE proteins, we show that bacterial hook can be divided in two distinct parts. The first part comprises domains that are found in all FlgE proteins and that will make the basic structure of the hook that is common to all flagellated bacteria. The second part, hyper-variable both in size and structure, will be bacteria dependent. To have a better understanding of the C. jejuni hook, we show that a special strain of Salmonella enterica, which was designed to encode a gene of flgE that has the extra domains found in FlgE from C. jejuni, is fully motile. It seems that no matter the size of the hook protein, the hook will always have a structure made of 11 protofilaments.
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