Fimbrial usher protein explained
The fimbrial usher protein is involved in biogenesis of the pilus in Gram-negative bacteria. The biogenesis of some fimbriae (or pili) requires a two-component assembly and transport system which is composed of a periplasmic chaperone and a pore-forming outer membrane protein which has been termed a molecular 'usher'; this is the chaperone-usher pathway.[1] [2] [3]
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[4] 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).[5] 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.
Notes and References
- Hultgren SJ, Jacob-Dubuisson F, Striker R . Chaperone-assisted self-assembly of pili independent of cellular energy . J. Biol. Chem. . 269 . 17 . 12447–12455 . 1994 . 10.1016/S0021-9258(18)99895-9 . 7909802 . free .
- Schifferli DM, Alrutz MA . Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli . J. Bacteriol. . 176 . 4 . 1099–1110 . 1994 . 10.1128/JB.176.4.1099-1110.1994 . 7906265 . 205162.
- Saier Jr MH, Van Rosmalen M . Structural and evolutionary relationships between two families of bacterial extracytoplasmic chaperone proteins which function cooperatively in fimbrial assembly . Res. Microbiol. . 144 . 7 . 507–527 . 1993 . 7906046 . 10.1016/0923-2508(93)90001-I. free .
- Capitani G, Eidam O, Grütter MG . 2006 . Evidence for a novel domain of bacterial outer membrane ushers . Proteins . 65 . 4. 816–23 . 10.1002/prot.21147 . 17066380 . 28766740 .
- 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 . 10.1038/nature10109 . 21637253 . 3162478.