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6RGV

Truncated FljB phase 2 flagellin

Summary for 6RGV
Entry DOI10.2210/pdb6rgv/pdb
Related1IO1
DescriptorFlagellin (2 entities in total)
Functional Keywordsflagellum, methylation, bacterial motility, cell adhesion, structural protein
Biological sourceSalmonella typhimurium (strain SL1344)
Total number of polymer chains1
Total formula weight44605.57
Authors
Lunelli, M.,Lokareddy, R.K.,Kolbe, M. (deposition date: 2019-04-17, release date: 2020-03-11, Last modification date: 2024-01-24)
Primary citationHorstmann, J.A.,Lunelli, M.,Cazzola, H.,Heidemann, J.,Kuhne, C.,Steffen, P.,Szefs, S.,Rossi, C.,Lokareddy, R.K.,Wang, C.,Lemaire, L.,Hughes, K.T.,Uetrecht, C.,Schluter, H.,Grassl, G.A.,Stradal, T.E.B.,Rossez, Y.,Kolbe, M.,Erhardt, M.
Methylation of Salmonella Typhimurium flagella promotes bacterial adhesion and host cell invasion.
Nat Commun, 11:2013-2013, 2020
Cited by
PubMed Abstract: The long external filament of bacterial flagella is composed of several thousand copies of a single protein, flagellin. Here, we explore the role played by lysine methylation of flagellin in Salmonella, which requires the methylase FliB. We show that both flagellins of Salmonella enterica serovar Typhimurium, FliC and FljB, are methylated at surface-exposed lysine residues by FliB. A Salmonella Typhimurium mutant deficient in flagellin methylation is outcompeted for gut colonization in a gastroenteritis mouse model, and methylation of flagellin promotes bacterial invasion of epithelial cells in vitro. Lysine methylation increases the surface hydrophobicity of flagellin, and enhances flagella-dependent adhesion of Salmonella to phosphatidylcholine vesicles and epithelial cells. Therefore, posttranslational methylation of flagellin facilitates adhesion of Salmonella Typhimurium to hydrophobic host cell surfaces, and contributes to efficient gut colonization and host infection.
PubMed: 32332720
DOI: 10.1038/s41467-020-15738-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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