You can manage bookmarks using lists, please log in to your user account for this.
Media type:
E-Article
Title:
Amide bonds assemble pili on the surface of bacilli
Contributor:
Budzik, Jonathan M.;
Marraffini, Luciano A.;
Souda, Puneet;
Whitelegge, Julian P.;
Faull, Kym F.;
Schneewind, Olaf
Published:
Proceedings of the National Academy of Sciences, 2008
Published in:
Proceedings of the National Academy of Sciences, 105 (2008) 29, Seite 10215-10220
Language:
English
DOI:
10.1073/pnas.0803565105
ISSN:
0027-8424;
1091-6490
Origination:
Footnote:
Description:
Pilin precursors are the building blocks of pili on the surface of Gram-positive bacteria; however, the assembly mechanisms of these adhesive fibers are unknown. Here, we describe the chemical bonds that assemble BcpA pilin subunits on the surface ofBacillus cereus. Sortase D cleaves BcpA precursor between the threonine (T) and the glycine (G) residues of its LPXTG sorting signal and catalyzes formation of an amide bond between threonine (T) of the sorting signal and lysine (K) in the YPKN motif of another BcpA subunit. Three CNA B domains of BcpA generate intramolecular amide bonds, and one of these contributes also to pilus formation. Conservation of catalysts and structural elements in pilin precursors in Gram-positive bacteria suggests a universal mechanism of fiber assembly.