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Fimbrial usher protein : ウィキペディア英語版 | Fimbrial usher protein
The fimbrial usher protein is involved in biogenesis of the pilus in Gram-negative bacteria. The biogenesis of fimbriae (or pili) requires a two-component assembly and transport system which is composed of a periplasmic chaperone and an outer membrane protein which has been termed a molecular 'usher'. The usher protein has a molecular weight ranging from 86 to 100 kDa and is composed of a membrane-spanning 24-stranded beta barrel domain, reminiscent of porins, and of four periplasmic soluble domains: an N-terminal one of about 120 residues (NTD),〔 a 'middle' domain of about 80 residues〔Capitani G, Eidam O, Grütter MG (2006) (Evidence for a novel domain of bacterial outer membrane ushers. ) ''Proteins'' 65 (4):816-23. PMID 17066380〕 located as a soluble insertion within the beta barrel region of the sequence (plug domain) and two IG-like domains (each about 80 residues long) at the C-terminus (CTD1 and CTD2).〔Phan G, Remaut H, Wang T, Allen WJ, Pirker KF, Lebedev A et al. (2011) (Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. ) ''Nature'' 474 (7349):49-53. PMID 21637253〕 Although the degree of sequence similarity of these proteins is not very high they share a number of characteristics. One of these is the presence of two pairs of disulfide bond-forming cysteines, the first one located in the NTD and the second in CTD2. The best conserved region of the sequence corresponds to the plug domain. ==References==
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