Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 105, Issue 29, Pages 10215-10220Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0803565105
Keywords
CNA B domain; LPXTG sorting signal; sortase; YPKN motif
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Funding
- NIAID NIH HHS [U54 AI057153, R01 AI038897, AI38897, R01 AI069227, 1-U54-AI-057153, AI69227] Funding Source: Medline
- NIGMS NIH HHS [GM07281, T32 GM007281] Funding Source: Medline
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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 of Bacillus 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.
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