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Flagellin
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== Structure == [[Image:EMpylori.jpg|thumb|''[[Helicobacter pylori]]'' electron micrograph, showing multiple [[flagella]] on the cell surface]] The structure of flagellin is responsible for the [[helix|helical]] shape of the flagellar filament, which is important for its proper function.<ref name="steiner">{{cite journal | vauthors = Steiner TS | title = How flagellin and toll-like receptor 5 contribute to enteric infection | journal = Infection and Immunity | volume = 75 | issue = 2 | pages = 545β52 | date = February 2007 | pmid = 17118981 | pmc = 1828527 | doi = 10.1128/IAI.01506-06 }}</ref> It is transported through the center of the filament to the tip where it [[polymerases]] spontaneously into a part of the filament. In ''[[E. coli]]'' it is unfolded by the flagellar secretion chaperone FliS ({{UniProt|P26608}}) during transport.<ref name=NBK6250>{{cite book |url=https://www.ncbi.nlm.nih.gov/books/NBK6250 |title=Structure, Function and Assembly of Flagellar Axial Proteins | vauthors = Vonderviszt F, Keiichi N |publisher=Madame Curie Bioscience Database |location=Austin, TX|year=2013 }}</ref> The filament is made up of eleven smaller "protofilaments", nine of which contains flagellin in the L-type shape and the other two in the R-type shape.<ref>{{cite journal | vauthors = Maki-Yonekura S, Yonekura K, Namba K | title = Conformational change of flagellin for polymorphic supercoiling of the flagellar filament | journal = Nature Structural & Molecular Biology | volume = 17 | issue = 4 | pages = 417β22 | date = April 2010 | pmid = 20228803 | doi = 10.1038/nsmb.1774 | s2cid = 31915502 }}</ref> The helical [[amino terminus|N-]] and [[carboxyl terminus|C-termini]] of flagellin form the inner core of the flagellin protein, and is responsible for flagellin's ability to [[polymer]]ize into a filament. The middle residues make up the outer surface of the flagellar filament. While the termini of the protein are quite similar among all bacterial flagellins, the middle portion is wildly variable and can be absent in some species. The flagellin domains are numbered from the helical core (D0/D1) to the outside (D2, ...); when viewed from the amino-acid sequence, D0/D1 appears on the two termini. Flagellin-like structural proteins are found in other portions of the flagellum, such as the hook (flgE; {{UniProt|P75937}}), the rod at the base, and the cap at the top.<ref>{{cite journal | vauthors = Imada K | title = Bacterial flagellar axial structure and its construction | journal = Biophysical Reviews | volume = 10 | issue = 2 | pages = 559β570 | date = April 2018 | pmid = 29235079 | pmc = 5899737 | doi = 10.1007/s12551-017-0378-z }}</ref> The middle part of Β ''E. coli'' (and related) flagellin, D3, displays a [[beta-folium]] fold and appears to maintain flagellar stability.<ref>{{cite journal | vauthors = Samatey FA, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, Yamamoto M, Namba K | title = Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling | journal = Nature | volume = 410 | issue = 6826 | pages = 331β7 | date = March 2001 | pmid = 11268201 | doi = 10.1038/35066504 | bibcode = 2001Natur.410..331S | s2cid = 4416455 }}</ref>
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